Journal articles: 'Npl3'

1

Henry, Michael, Christina Z. Borland, Mark Bossie, and Pamela A. Silver. "Potential RNA Binding Proteins in Saccharomyces cerevisiae Identified as Suppressors of Temperature-Sensitive Mutations in NPL3." Genetics 142, no. 1 (January 1, 1996): 103–15. http://dx.doi.org/10.1093/genetics/142.1.103.

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The NPL3 gene of the yeast Saccharomyces cerevisiae encodes a protein with similarity to heterogeneous nuclear ribonucleoproteins (hnRNPs). Npl3p has been implicated in many nuclear-related events including RNA export, protein import, and rRNA processing. Several temperature-sensitive alleles of NPL3 have been isolated. We now report the sequence of these alleles. For one allele, npl3-1, four complementation groups of suppressors have been isolated. The cognate genes for the two recessive mutants were cloned. One of these is the previously known RNA15, which, like NPL3, also encodes a protein with similarity to the vertebrate hnRNP A/B protein family. The other suppressor corresponds to a newly defined gene we term HRP1, which also encodes a protein with similarity to the hnRNP A/B proteins of vertebrates. Mutations in HRP1 suppress all npl3 temperature-sensitive alleles but do not bypass an npl3 null allele. We show that HRP1 is essential for cell growth and that the corresponding protein is located in the nucleus. The discovery of two hnRNP homologues that can partially suppress the function of Npl3p, also an RNA binding protein, will be discussed in terms of the possible roles for Npl3p in RNA metabolism.

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Nelson, M. K., T. Kurihara, and P. A. Silver. "Extragenic suppressors of mutations in the cytoplasmic C terminus of SEC63 define five genes in Saccharomyces cerevisiae." Genetics 134, no. 1 (May 1, 1993): 159–73. http://dx.doi.org/10.1093/genetics/134.1.159.

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Abstract Mutations in the SEC63 gene of Saccharomyces cerevisiae affect both nuclear protein localization and translocation of proteins into the endoplasmic reticulum. We now report the isolation of suppressors of sec63-101 (formerly npl1-1), a temperature-sensitive allele of SEC63. Five complementation groups of extragenic mutations, son1-son5 (suppressor of npl1-1), were identified among the recessive suppressors. The son mutations are specific to SEC63, are not bypass suppressors, and are not new alleles of previously identified secretory (SEC61, SEC62, KAR2) or nuclear protein localization genes (NPL3, NPL4, NPL6). son1 mutations show regional specificity of suppression of sec63 alleles. At low temperatures, son1 mutants grow slowly and show partial mislocalization of nuclear antigens. The SON1 gene maps to chromosome IV and encodes a nuclear protein of 531 amino acids that contains two acidic stretches and a putative nuclear localization sequence. We show that son1 mutations suppress sec63-101 by elimination of Son1p function.

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Henry, M. F., and P. A. Silver. "A novel methyltransferase (Hmt1p) modifies poly(A)+-RNA-binding proteins." Molecular and Cellular Biology 16, no. 7 (July 1996): 3668–78. http://dx.doi.org/10.1128/mcb.16.7.3668.

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RNA-binding proteins play many essential roles in the metabolism of nuclear pre-mRNA. As such, they demonstrate a myriad of dynamic behaviors and modifications. In particular, heterogeneous nuclear ribonucleoproteins (hnRNPs) contain the bulk of methylated arginine residues in eukaryotic cells. We have identified the first eukaryotic hnRNP-specific methyltransferase via a genetic screen for proteins that interact with an abundant poly(A)+-RNA-binding protein termed Npl3p. We have previously shown that npl3-1 mutants are temperature sensitive for growth and defective for export of mRNA from the nucleus. New mutants in interacting genes were isolated by their failure to survive in the presence of the npl3-1 allele. Four alleles of the same gene were identified in this manner. Cloning of the cognate gene revealed an encoded protein with similarity to methyltransferases that was termed HMT1 for hnRNP methyltransferase. HMT1 is not required for normal cell viability except when NPL3 is also defective. The Hmt1 protein is located in the nucleus. We demonstrate that Npl3p is methylated by Hmt1p both in vivo and in vitro. These findings now allow further exploration of the function of this previously uncharacterized class of enzymes.

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Lund, Mette K., Tracy L. Kress, and Christine Guthrie. "Autoregulation of Npl3, a Yeast SR Protein, Requires a Novel Downstream Region and Serine Phosphorylation." Molecular and Cellular Biology 28, no. 11 (April 7, 2008): 3873–81. http://dx.doi.org/10.1128/mcb.02153-07.

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ABSTRACT Npl3 is an SR-like protein with documented roles in mRNA export and transcription termination. Maintaining appropriate levels of Npl3 protein is critical for cell survival. Here we show that Npl3 negatively regulates its own expression via modulation of its mRNA levels. By creating gene chimeras, we demonstrate that the region downstream of the coding sequence of Npl3 is necessary and sufficient to confer regulation. The use of different polyadenylation sites in this region results in at least two stable RNAs; read-through of these sites causes the formation of 3′-extended RNAs that are highly unstable and therefore largely unproductive. Increasing the amount of Npl3 protein promotes read-through. Notably, the loss of Npl3 phosphorylation promotes the use of the productive polyadenylation sites, resulting in elevated levels of Npl3 protein. We propose that proper levels of Npl3 protein are achieved by a negative feedback loop in which phosphorylated Npl3 suppresses efficient recognition of the productive processing signals in its own transcript.

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Loo, S., P. Laurenson, M. Foss, A. Dillin, and J. Rine. "Roles of ABF1, NPL3, and YCL54 in silencing in Saccharomyces cerevisiae." Genetics 141, no. 3 (November 1, 1995): 889–902. http://dx.doi.org/10.1093/genetics/141.3.889.

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Abstract A sensitized genetic screen was carried out to identify essential genes involved in silencing in Saccharomyces cerevisiae. This screen identified temperature-sensitive alleles of ORC2 and ORC5, as described elsewhere, and ABF1, NPL3, and YCL54, as described here. Alleles of ABF1 that caused silencing defects provided the genetic proof of Abflp's role in silencing. The roles of Npl3p and Ycl54p are less clear. These proteins did not act exclusively through any one of the three protein binding sites of the HMR-E silencer. Unlike the orc2, orc5, and abf1 mutations that were isolated in the same (or a similar) screen for silencing mutants, neither temperature-sensitive mutation in NPL3 or YCL54 caused overt replication defects.

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Sandhu, Rima, Aniketa Sinha, and Ben Montpetit. "The SR-protein Npl3 is an essential component of the meiotic splicing regulatory network in Saccharomyces cerevisiae." Nucleic Acids Research 49, no. 5 (February 12, 2021): 2552–68. http://dx.doi.org/10.1093/nar/gkab071.

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Abstract The meiotic gene expression program in Saccharomyces cerevisiae involves regulated splicing of meiosis-specific genes via multiple splicing activators (e.g. Mer1, Nam8, Tgs1). Here, we show that the SR protein Npl3 is required for meiotic splicing regulation and is essential for proper execution of the meiotic cell cycle. The loss of Npl3, though not required for viability in mitosis, caused intron retention in meiosis-specific transcripts, inefficient meiotic double strand break processing and an arrest of the meiotic cell cycle. The targets of Npl3 overlapped in some cases with other splicing regulators, while also having unique target transcripts that were not shared. In the absence of Npl3, splicing defects for three transcripts (MER2, HOP2 and SAE3) were rescued by conversion of non-consensus splice sites to the consensus sequence. Methylation of Npl3 was further found to be required for splicing Mer1-dependent transcripts, indicating transcript-specific mechanisms by which Npl3 supports splicing. Together these data identify an essential function for the budding yeast SR protein Npl3 in meiosis as part of the meiotic splicing regulatory network.

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7

Bossie, M. A., C. DeHoratius, G. Barcelo, and P. Silver. "A mutant nuclear protein with similarity to RNA binding proteins interferes with nuclear import in yeast." Molecular Biology of the Cell 3, no. 8 (August 1992): 875–93. http://dx.doi.org/10.1091/mbc.3.8.875.

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We have isolated mutants of the yeast Saccharomyces cerevisiae that are defective in localization of nuclear proteins. Chimeric proteins containing the nuclear localization sequence from SV40 large T-antigen fused to the N-terminus of the mitochondrial F1 beta-ATPase are localized to the nucleus. Npl (nuclear protein localization) mutants were isolated by their ability to grow on glycerol as a consequence of no longer exclusively targeting SV40-F1 beta-ATPase to the nucleus. All mutants with defects in localization of nucleolar proteins and histones are temperature sensitive for growth at 36 degrees C. Seven alleles of NPL3 and single alleles of several additional genes were isolated. NPL3 mutants were studied in detail. NPL3 encodes a nuclear protein with an RNA recognition motif and similarities to a family of proteins involved in RNA metabolism. Our genetic analysis indicates that NPL3 is essential for normal cell growth; cells lacking NPL3 are temperature sensitive for growth but do not exhibit a defect in localization of nuclear proteins. Taken together, these results indicate that the mutant forms of Npl3 protein isolated by this procedure are interfering with nuclear protein uptake in a general manner.

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8

Rollenhagen, Christiane, Christine A. Hodge, and Charles N. Cole. "Following Temperature Stress, Export of Heat Shock mRNA Occurs Efficiently in Cells with Mutations in Genes Normally Important for mRNA Export." Eukaryotic Cell 6, no. 3 (January 26, 2007): 505–13. http://dx.doi.org/10.1128/ec.00317-06.

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ABSTRACT Heat shock leads to accumulation of polyadenylated RNA in nuclei of Saccharomyces cerevisiae cells, transcriptional induction of heat shock genes, and efficient export of polyadenylated heat shock mRNAs. These studies were conducted to examine the requirements for export of mRNA following heat shock. We used in situ hybridization to detect SSA4 mRNA (encoding Hsp70) and flow cytometry to measure the amount of Ssa4p-green fluorescent protein (GFP) produced following heat shock. Npl3p and Yra1p are mRNA-binding proteins recruited to nascent mRNAs and are essential for proper mRNA biogenesis and export. Heat shock mRNA was exported efficiently in temperature-sensitive npl3, yra1, and npl3 yra1 mutant strains. Nevertheless, Yra1p was recruited to heat shock mRNA, as were Nab2p and Npl3p. Interestingly, Yra1p was not recruited to heat shock mRNA in yra1-1 cells, suggesting that Npl3p is required for recruitment of Yra1p. The THO complex, which functions in transcription elongation and in recruitment of Yra1p, was not required for heat shock mRNA export, although normal mRNA export is impaired in growing cells lacking THO complex proteins. Taken together, these studies indicate that export following heat shock depends upon fewer factors than does mRNA export in growing cells. Furthermore, even though some mRNA-binding proteins are dispensable for efficient export of heat shock mRNA, those that are present in nuclei of heat shocked cells were recruited to heat shock mRNA.

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9

Flach, J., M. Bossie, J. Vogel, A. Corbett, T. Jinks, D. A. Willins, and P. A. Silver. "A yeast RNA-binding protein shuttles between the nucleus and the cytoplasm." Molecular and Cellular Biology 14, no. 12 (December 1994): 8399–407. http://dx.doi.org/10.1128/mcb.14.12.8399-8407.1994.

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RNA-binding proteins have been suggested to move in association with RNA as it leaves the nucleus. The NPL3 gene of the yeast Saccharomyces cerevisiae encodes in nuclear protein with consensus RNA-binding motifs and similarity to heterogeneous nuclear ribonucleoproteins and members of the S/R protein family. We show that although Npl3 is located in the nucleus, it can shuttle between nuclei in yeast heterokaryons. In contrast, other nucleus-targeted proteins do not leave the nucleus under similar conditions. Mutants missing the RNA-binding motifs or the N terminus are still capable of shuttling in and out of the nucleus. Npl3 mutants missing the C terminus fail to localize to the nucleus. Overproduction of Npl3 in wild-type cells shows cell growth. This toxicity depends on the presence of series of unique repeats in the N terminus and localization to the nucleus. We suggest that the properties of Npl3 are consistent with it being involved in export of RNAs from the nucleus.

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10

Flach, J., M. Bossie, J. Vogel, A. Corbett, T. Jinks, D. A. Willins, and P. A. Silver. "A yeast RNA-binding protein shuttles between the nucleus and the cytoplasm." Molecular and Cellular Biology 14, no. 12 (December 1994): 8399–407. http://dx.doi.org/10.1128/mcb.14.12.8399.

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RNA-binding proteins have been suggested to move in association with RNA as it leaves the nucleus. The NPL3 gene of the yeast Saccharomyces cerevisiae encodes in nuclear protein with consensus RNA-binding motifs and similarity to heterogeneous nuclear ribonucleoproteins and members of the S/R protein family. We show that although Npl3 is located in the nucleus, it can shuttle between nuclei in yeast heterokaryons. In contrast, other nucleus-targeted proteins do not leave the nucleus under similar conditions. Mutants missing the RNA-binding motifs or the N terminus are still capable of shuttling in and out of the nucleus. Npl3 mutants missing the C terminus fail to localize to the nucleus. Overproduction of Npl3 in wild-type cells shows cell growth. This toxicity depends on the presence of series of unique repeats in the N terminus and localization to the nucleus. We suggest that the properties of Npl3 are consistent with it being involved in export of RNAs from the nucleus.

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11

Singleton, D. R., S. Chen, M. Hitomi, C. Kumagai, and A. M. Tartakoff. "A yeast protein that bidirectionally affects nucleocytoplasmic transport." Journal of Cell Science 108, no. 1 (January 1, 1995): 265–72. http://dx.doi.org/10.1242/jcs.108.1.265.

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We have identified a temperature-sensitive mutant of Saccharomyces cerevisiae (npl3) that accumulates polyadenylated RNA in the nucleus at 37 degrees C, as judged by in situ hybridization. The strong nuclear signal is not simply due to increased cytoplasmic turnover of mRNA, as reincubation at 37 degrees C with an RNA polymerase inhibitor shows no diminution in the in situ signal. Over several hours at 37 degrees C, the average poly(A) tail length increases and a characteristic ultrastructural alteration of the nucleoplasm occurs. Cloning and sequencing indicate that the corresponding gene is NPL3/NOP3, which codes for a nucleolar/nuclear protein implicated in protein import into the nucleus (Bossie et al. (1992). Mol. Biol. Cell 3, 875–893) and in rRNA maturation (Russell and Tollervey (1992). J. Cell Biol. 119, 737–747). NPL3 includes bipartite RNA recognition motifs (RRM) and a Gly-Arg repeat domain, as in several nucleolar proteins. A point mutation adjacent to one of the RRM has been identified in the ts copy of the gene. Although this protein is not concentrated in nuclear pores, NPL3 is implicated in both import and export from the nucleus. Judging from the site of the npl3 mutation and since the block in RNA export can be detected prior to an obvious nuclear import defect in npl3, the defect in RNA export may be primary. Since other mutants that interrupt RNA export do not block protein import, the NPL3 protein itself appears to be implicated in protein import.

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12

McBride, Anne E., Cecilia Zurita-Lopez, Anthony Regis, Emily Blum, Ana Conboy, Shannon Elf, and Steven Clarke. "Protein Arginine Methylation in Candida albicans: Role in Nuclear Transport." Eukaryotic Cell 6, no. 7 (May 4, 2007): 1119–29. http://dx.doi.org/10.1128/ec.00074-07.

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ABSTRACT Protein arginine methylation plays a key role in numerous eukaryotic processes, such as protein transport and signal transduction. In Candida albicans, two candidate protein arginine methyltransferases (PRMTs) have been identified from the genome sequencing project. Based on sequence comparison, C. albicans candidate PRMTs display similarity to Saccharomyces cerevisiae Hmt1 and Rmt2. Here we demonstrate functional homology of Hmt1 between C. albicans and S. cerevisiae: CaHmt1 supports growth of S. cerevisiae strains that require Hmt1, and CaHmt1 methylates Npl3, a major Hmt1 substrate, in S. cerevisiae. In C. albicans strains lacking CaHmt1, asymmetric dimethylarginine and ω-monomethylarginine levels are significantly decreased, indicating that Hmt1 is the major C. albicans type I PRMT1. Given the known effects of type I PRMTs on nuclear transport of RNA-binding proteins, we tested whether Hmt1 affects nuclear transport of a putative Npl3 ortholog in C. albicans. CaNpl3 allows partial growth of S. cerevisiae npl3Δ strains, but its arginine-glycine-rich C terminus can fully substitute for that of ScNpl3 and also directs methylation-sensitive association with ScNpl3. Expression of green fluorescent protein-tagged CaNpl3 proteins in C. albicans strains with and without CaHmt1 provides evidence for CaHmt1 facilitating export of CaNpl3 in this fungus. We have also identified the C. albicans Rmt2, a type IV fungus- and plant-specific PRMT, by amino acid analysis of an rmt2Δ/rmt2Δ strain, as well as biochemical evidence for additional cryptic PRMTs.

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13

Windgassen, Merle, Dorothée Sturm, Iván J. Cajigas, Carlos I. González, Matthias Seedorf, Holger Bastians, and Heike Krebber. "Yeast Shuttling SR Proteins Npl3p, Gbp2p, and Hrb1p Are Part of the Translating mRNPs, and Npl3p Can Function as a Translational Repressor." Molecular and Cellular Biology 24, no. 23 (December 1, 2004): 10479–91. http://dx.doi.org/10.1128/mcb.24.23.10479-10491.2004.

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ABSTRACT A major challenge in current molecular biology is to understand how sequential steps in gene expression are coupled. Recently, much attention has been focused on the linkage of transcription, processing, and mRNA export. Here we describe the cytoplasmic rearrangement for shuttling mRNA binding proteins in Saccharomyces cerevisiae during translation. While the bulk of Hrp1p, Nab2p, or Mex67p is not associated with polysome containing mRNAs, significant amounts of the serine/arginine (SR)-type shuttling mRNA binding proteins Npl3p, Gbp2p, and Hrb1p remain associated with the mRNA-protein complex during translation. Interestingly, a prolonged association of Npl3p with polysome containing mRNAs results in translational defects, indicating that Npl3p can function as a negative translational regulator. Consistent with this idea, a mutation in NPL3 that slows down translation suppresses growth defects caused by the presence of translation inhibitors or a mutation in eIF5A. Moreover, using sucrose density gradient analysis, we provide evidence that the import receptor Mtr10p, but not the SR protein kinase Sky1p, is involved in the timely regulated release of Npl3p from polysome-associated mRNAs. Together, these data shed light onto the transformation of an exporting to a translating mRNP.

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Xu, Chong, and Michael F. Henry. "Nuclear Export of hnRNP Hrp1p and Nuclear Export of hnRNP Npl3p Are Linked and Influenced by the Methylation State of Npl3p." Molecular and Cellular Biology 24, no. 24 (December 15, 2004): 10742–56. http://dx.doi.org/10.1128/mcb.24.24.10742-10756.2004.

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ABSTRACT Eukaryotic mRNA processing and export are mediated by a series of complexes composed of heterogeneous nuclear ribonucleoproteins (hnRNPs). Many of these hnRNPs are methylated at arginine residues within their RGG domains. Although cellular arginine methylation is required for the efficient nuclear export of several hnRNPs, its role in this process is unknown. To address this question, we replaced the methylated RGG tripeptides of two hnRNPs, Npl3p and Hrp1p, with KGG. We found that these substitutions specifically abolish their methylation but have different effects on their nuclear export activity. Although the efficient export of Hrp1p requires cellular methyltransferase activity, the modification of Hrp1p itself is dispensable. In contrast, we found that Npl3 arginine methylation not only facilitates its own export but also is required for Hrp1p to efficiently exit the nucleus. Consistent with this observation, we found that Npl3p and Hrp1p exist in a ribonucleoprotein complex. We provide the first evidence that the arginine methylation of a particular protein directly affects its activity. Efficient export does not require methylation per se, but unmethylated arginine residues lead to retention of hnRNPs. Thus, arginine methylation serves to mask the Npl3p RGG domain for efficient ribonucleoprotein export.

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Wong, Chi-Ming, Hongfang Qiu, Cuihua Hu, Jinsheng Dong, and Alan G. Hinnebusch. "Yeast Cap Binding Complex Impedes Recruitment of Cleavage Factor IA to Weak Termination Sites." Molecular and Cellular Biology 27, no. 18 (July 16, 2007): 6520–31. http://dx.doi.org/10.1128/mcb.00733-07.

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ABSTRACT Nuclear cap binding complex (CBC) is recruited cotranscriptionally and stimulates spliceosome assembly on nascent mRNAs; however, its possible functions in regulating transcription elongation or termination were not well understood. We show that, while CBC appears to be dispensable for normal rates and processivity of elongation by RNA polymerase II (Pol II), it plays a direct role in preventing polyadenylation at weak termination sites. Similarly to Npl3p, with which it interacts, CBC suppresses the weak terminator of the gal10-Δ56 mutant allele by impeding recruitment of termination factors Pcf11p and Rna15p (subunits of cleavage factor IA [CF IA]) and does so without influencing Npl3p occupancy at the termination site. Importantly, deletion of CBC subunits or NPL3 also increases termination at a naturally occurring weak poly(A) site in the RNA14 coding sequences. We also show that CBC is most likely recruited directly to the cap of nascent transcripts rather than interacting first with transcriptional activators or the phosphorylated C-terminal domain of Pol II. Thus, our findings illuminate the mechanism of CBC recruitment and extend its function in Saccharomyces cerevisiae beyond mRNA splicing and degradation of aberrant nuclear mRNAs to include regulation of CF IA recruitment at poly(A) selection sites.

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16

Dermody, Jessica L., Jonathan M. Dreyfuss, Judit Villén, Babatunde Ogundipe, Steven P. Gygi, Peter J. Park, Alfred S. Ponticelli, Claire L. Moore, Stephen Buratowski, and Miriam E. Bucheli. "Unphosphorylated SR-Like Protein Npl3 Stimulates RNA Polymerase II Elongation." PLoS ONE 3, no. 9 (September 26, 2008): e3273. http://dx.doi.org/10.1371/journal.pone.0003273.

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17

Estrella, Luis A., Miles F. Wilkinson, and Carlos I. González. "The Shuttling Protein Npl3 Promotes Translation Termination Accuracy in Saccharomyces cerevisiae." Journal of Molecular Biology 394, no. 3 (December 2009): 410–22. http://dx.doi.org/10.1016/j.jmb.2009.08.067.

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18

Moehle, Erica A., Colm J. Ryan, Nevan J. Krogan, Tracy L. Kress, and Christine Guthrie. "The Yeast SR-Like Protein Npl3 Links Chromatin Modification to mRNA Processing." PLoS Genetics 8, no. 11 (November 29, 2012): e1003101. http://dx.doi.org/10.1371/journal.pgen.1003101.

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19

Aubol, Brandon E., Leslie Ungs, Randy Lukasiewicz, Gourisankar Ghosh, and Joseph A. Adams. "Chemical Clamping Allows for Efficient Phosphorylation of the RNA Carrier Protein Npl3." Journal of Biological Chemistry 279, no. 29 (May 15, 2004): 30182–88. http://dx.doi.org/10.1074/jbc.m402797200.

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20

Baierlein, C., A. Hackmann, T. Gross, L. Henker, F. Hinz, and H. Krebber. "Monosome Formation during Translation Initiation Requires the Serine/Arginine-Rich Protein Npl3." Molecular and Cellular Biology 33, no. 24 (October 7, 2013): 4811–23. http://dx.doi.org/10.1128/mcb.00873-13.

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21

Santos-Pereira, J. M., A. B. Herrero, M. L. Garcia-Rubio, A. Marin, S. Moreno, and A. Aguilera. "The Npl3 hnRNP prevents R-loop-mediated transcription-replication conflicts and genome instability." Genes & Development 27, no. 22 (November 15, 2013): 2445–58. http://dx.doi.org/10.1101/gad.229880.113.

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Hackmann, Alexandra, Thomas Gross, Claudia Baierlein, and Heike Krebber. "The mRNA export factor Npl3 mediates the nuclear export of large ribosomal subunits." EMBO reports 12, no. 10 (October 2011): 1024–31. http://dx.doi.org/10.1038/embor.2011.155.

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Kress, Tracy L., Nevan J. Krogan, and Christine Guthrie. "A Single SR-like Protein, Npl3, Promotes Pre-mRNA Splicing in Budding Yeast." Molecular Cell 32, no. 5 (December 2008): 727–34. http://dx.doi.org/10.1016/j.molcel.2008.11.013.

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Bucheli, Miriam E., and Stephen Buratowski. "Npl3 is an antagonist of mRNA 3′ end formation by RNA polymerase II." EMBO Journal 24, no. 12 (May 19, 2005): 2150–60. http://dx.doi.org/10.1038/sj.emboj.7600687.

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Santos-Pereira, José M., Ana B. Herrero, Sergio Moreno, and Andrés Aguilera. "Npl3, a new link between RNA-binding proteins and the maintenance of genome integrity." Cell Cycle 13, no. 10 (April 2, 2014): 1524–29. http://dx.doi.org/10.4161/cc.28708.

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Holmes, Rebecca K., Alex C. Tuck, Chenchen Zhu, Hywel R. Dunn-Davies, Grzegorz Kudla, Sandra Clauder-Munster, Sander Granneman, Lars M. Steinmetz, Christine Guthrie, and David Tollervey. "Loss of the Yeast SR Protein Npl3 Alters Gene Expression Due to Transcription Readthrough." PLOS Genetics 11, no. 12 (December 22, 2015): e1005735. http://dx.doi.org/10.1371/journal.pgen.1005735.

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27

Bucheli, M. E., X. He, C. D. Kaplan, C. L. Moore, and S. Buratowski. "Polyadenylation site choice in yeast is affected by competition between Npl3 and polyadenylation factor CFI." RNA 13, no. 10 (August 13, 2007): 1756–64. http://dx.doi.org/10.1261/rna.607207.

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Deka, Pritilekha, Miriam E. Bucheli, Claire Moore, Stephen Buratowski, and Gabriele Varani. "Structure of the Yeast SR Protein Npl3 and Interaction with mRNA 3′-End Processing Signals." Journal of Molecular Biology 375, no. 1 (January 2008): 136–50. http://dx.doi.org/10.1016/j.jmb.2007.09.029.

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Benedicta OWONYE and Godwin OBONOFIEMRO. "DETERMINANTS OF NON-PERFORMING LOANS IN THE NIGERIA BANKING INDUSTRY." International Journal of Management & Entrepreneurship Research 4, no. 11 (November 8, 2022): 428–40. http://dx.doi.org/10.51594/ijmer.v4i11.402.

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This study examined the determinants of non-performing loans (NPLs) in the Nigeria banking industry between the periods of 2011-2020. The specific objective of the study is to examine the relationship between the measures of bank specific variables [Bank Size (BS), Capital Adequacy (CA), Profitability (PROF), Bank Age (BA), Liquidity (LIQ) and Loan to Total Assets (LTA)] and [NPLs proxy with Non Performing Loans Ratio (NPLR)] in Nigeria. The focus on the banks in Nigeria listed in the Nigeria Stock Exchange and the difficulty in assessing their annual reports and account of 10 banks were drawn out of the 18 deposit money banks (DMBs) for the study. The data for the study was gotten from the annual reports and accounts of the ten (10) banks on the basis of the variables under study and the data was analyzed using descriptive statistics, correlation and multiple regression analysis. The findings revealed that BS, CA and BA have significant effect on NPLR but the effect of BS and BA on NPR are negative while PROF have negative insignificant effect on NPLR of DMBs in Nigeria. This research found that determinants of NPLs have mix effect on NPLR in Nigeria. The findings suggested that BS in relation to total assets should put in consideration when granting loans and also, the DMBs in Nigeria should maintain and implement the capital adequacy policy enacted by the CBN. Keywords: Non-Performing Loans, Bank Size, Capital Adequacy, Profitability, Bank Age, and Liquidity.

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Colombo, Chiara Vittoria, Camilla Trovesi, Luca Menin, Maria Pia Longhese, and Michela Clerici. "The RNA binding protein Npl3 promotes resection of DNA double-strand breaks by regulating the levels of Exo1." Nucleic Acids Research 45, no. 11 (May 2, 2017): 6530–45. http://dx.doi.org/10.1093/nar/gkx347.

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McBride, Anne E., Jeffrey T. Cook, Elizabeth A. Stemmler, Kate L. Rutledge, Kelly A. McGrath, and Jeffrey A. Rubens. "Arginine Methylation of Yeast mRNA-binding Protein Npl3 Directly Affects Its Function, Nuclear Export, and Intranuclear Protein Interactions." Journal of Biological Chemistry 280, no. 35 (July 5, 2005): 30888–98. http://dx.doi.org/10.1074/jbc.m505831200.

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Muddukrishna, Bhavana, Christopher A. Jackson, and Michael C. Yu. "Protein arginine methylation of Npl3 promotes splicing of the SUS1 intron harboring non-consensus 5′ splice site and branch site." Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms 1860, no. 6 (June 2017): 730–39. http://dx.doi.org/10.1016/j.bbagrm.2017.04.001.

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33

Stochaj, U., M. A. Bossie, K. van Zee, A. M. Whalen, and P. A. Silver. "Analysis of conserved binding proteins for nuclear localization sequences." Journal of Cell Science 104, no. 1 (January 1, 1993): 89–95. http://dx.doi.org/10.1242/jcs.104.1.89.

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Correct targeting of nuclear proteins is mediated by nuclear localization sequences (NLS) which permit specific binding to the nucleus and subsequent translocation across the nuclear envelope via the nuclear pore complex. It is proposed that nuclear import is facilitated by NLS-receptors which reside in the cytoplasm and at the nuclear pore. These NLS-receptors could facilitate an early step of nuclear protein import, i.e. targeting and binding of nuclear proteins at the nuclear pore. We have generated anti-idiotype antibodies against the SV40 T-antigen nuclear localization sequence that allowed us to study NLS-binding proteins in a variety of different organisms. Proteins of similar size are recognized by these antibodies in yeast, Drosophila, rat and human cells. Cytological analysis indicates that the NLS-binding proteins reside in part at nuclear pores. One of the proteins recognized by anti-idiotype antibodies is identical to a previously identified NLS-binding protein. Using isolated yeast nuclei we demonstrate that the anti-idiotype antibodies compete for binding of nuclear proteins in vitro. We show that the yeast mutant npl3, which is defective in nuclear protein localization, has an altered distribution of antigens recognized by these anti-idiotype antibodies, at the semi-permissive temperature. Our results suggest that a set of proteins common to various eukaryotes recognizes nuclear localization sequences.

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Chen, Yin-Chu, Eric J. Milliman, Isabelle Goulet, Jocelyn Côté, Christopher A. Jackson, Jennifer A. Vollbracht, and Michael C. Yu. "Protein Arginine Methylation Facilitates Cotranscriptional Recruitment of Pre-mRNA Splicing Factors." Molecular and Cellular Biology 30, no. 21 (September 7, 2010): 5245–56. http://dx.doi.org/10.1128/mcb.00359-10.

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ABSTRACT Cotranscriptional recruitment of pre-mRNA splicing factors to their genomic targets facilitates efficient and ordered assembly of a mature messenger ribonucleoprotein particle (mRNP). However, how the cotranscriptional recruitment of splicing factors is regulated remains largely unknown. Here, we demonstrate that protein arginine methylation plays a novel role in regulating this process in Saccharomyces cerevisiae. Our data show that Hmt1, the major type I arginine methyltransferase, methylates Snp1, a U1 small nuclear RNP (snRNP)-specific protein, and that the mammalian Snp1 homolog, U1-70K, is likewise arginine methylated. Genome-wide localization analysis reveals that the deletion of the HMT1 gene deregulates the recruitment of U1 snRNP and its associated components to intron-containing genes (ICGs). In the same context, splicing factors acting downstream of U1 snRNP addition bind to a reduced number of ICGs. Quantitative measurement of the abundance of spliced target transcripts shows that these changes in recruitment result in an increase in the splicing efficiency of developmentally regulated mRNAs. We also show that in the absence of either Hmt1 or of its catalytic activity, an association between Snp1 and the SR-like protein Npl3 is substantially increased. Together, these data support a model whereby arginine methylation modulates dynamic associations between SR-like protein and pre-mRNA splicing factor to promote target specificity in splicing.

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Ariyachet, Chaiyaboot, Norma V. Solis, Yaoping Liu, Nemani V. Prasadarao, Scott G. Filler, and Anne E. McBride. "SR-Like RNA-Binding Protein Slr1 Affects Candida albicans Filamentation and Virulence." Infection and Immunity 81, no. 4 (February 4, 2013): 1267–76. http://dx.doi.org/10.1128/iai.00864-12.

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ABSTRACTCandida albicanscauses both mucosal and disseminated infections, and its capacity to grow as both yeast and hyphae is a key virulence factor. Hyphal formation is a type of polarized growth, and members of the SR (serine-arginine) family of RNA-binding proteins influence polarized growth of bothSaccharomyces cerevisiaeandAspergillus nidulans. Therefore, we investigated whether SR-like proteins affect filamentous growth and virulence ofC. albicans. BLAST searches withS. cerevisiaeSR-like protein Npl3 (ScNpl3) identified twoC. albicansproteins: CaNpl3, an apparent ScNpl3 ortholog, and Slr1, anotherSR-likeRNA-binding protein with no closeS. cerevisiaeortholog. Whereas ScNpl3 was critical for growth, deletion ofNPL3inC. albicansresulted in few phenotypic changes. In contrast, theslr1Δ/Δ mutant had a reduced growth ratein vitro, decreased filamentation, and impaired capacity to damage epithelial and endothelial cellsin vitro. Mice infected intravenously with theslr1Δ/Δ mutant strain had significantly prolonged survival compared to that of mice infected with the wild-type orslr1Δ/Δ mutant complemented withSLR1(slr1Δ/Δ+SLR1) strain, without a concomitant decrease in kidney fungal burden. Histopathology, however, revealed differential localization ofslr1Δ/Δ hyphal and yeast morphologies within the kidney. Mice infected withslr1Δ/Δ cells also had an increased brain fungal burden, which correlated with increased invasion of brain, but not umbilical vein, endothelial cellsin vitro. The enhanced brain endothelial cell invasion was likely due to the increased surface exposure of the Als3 adhesin onslr1Δ/Δ cells. Our results indicate that Slr1 is an SR-like protein that influencesC. albicansgrowth, filamentation, host cell interactions, and virulence.

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Smith, Daniela-Lee, Michael Götze, Tara K. Bartolec, Gene Hart-Smith, and Marc R. Wilkins. "Characterization of the Interaction between Arginine Methyltransferase Hmt1 and Its Substrate Npl3: Use of Multiple Cross-Linkers, Mass Spectrometric Approaches, and Software Platforms." Analytical Chemistry 90, no. 15 (July 13, 2018): 9101–8. http://dx.doi.org/10.1021/acs.analchem.8b01525.

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Markovich, Sarit, Aya Yekutiel, Itamar Shalit, Yona Shadkchan, and Nir Osherov. "Genomic Approach to Identification of Mutations Affecting Caspofungin Susceptibility in Saccharomyces cerevisiae." Antimicrobial Agents and Chemotherapy 48, no. 10 (October 2004): 3871–76. http://dx.doi.org/10.1128/aac.48.10.3871-3876.2004.

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ABSTRACT The antifungal agent caspofungin (CAS) specifically interferes with glucan synthesis and cell wall formation. To further study the cellular processes affected by CAS, we analyzed a Saccharomyces cerevisiae mutant collection (4,787 individual knockout mutations) to identify new genes affecting susceptibility to the drug. This collection was screened for increased CAS sensitivity (CAS-IS) or increased CAS resistance (CAS-IR). MICs were determined by the broth microdilution method. Disruption of 20 genes led to CAS-IS (four- to eightfold reductions in the MIC). Eleven of the 20 genes are involved in cell wall and membrane function, notably in the protein kinase C (PKC) integrity pathway (MID2, FKS1, SMI1, and BCK1), chitin and mannan biosynthesis (CHS3, CHS4, CHS7, and MNN10), and ergosterol biosynthesis (ERG5 and ERG6). Four of the 20 genes (TPO1, VPS65, VPS25, and CHC1) are involved in vacuole and transport functions, 3 of the 20 genes (CCR4, POP2, and NPL3) are involved in the control of transcription, and 2 of the 20 genes are of unknown function. Disruption of nine additional genes led to CAS-IR (a fourfold increase of MIC). Five of these nine genes (SLG1, ERG3, VRP1, CSG2, and CKA2) are involved in cell wall function and signal transduction, and two of the nine genes (VPS67 and SAC2) are involved in vacuole function. To assess the specificity of susceptibility to CAS, the MICs of amphotericin B, fluconazole, flucytosine, and calcofluor for the strains were tested. Seven of 20 CAS-IS strains (with disruption of FKS1, SMI1, BCK1, CHS4, ERG5, TPO1, and ILM1) and 1 of 9 CAS-IR strains (with disruption of SLG1) demonstrated selective susceptibility to CAS. To further explore the importance of PKC in CAS susceptibility, the activity of the PKC inhibitor staurosporine in combination with CAS was tested against eight Aspergillus clinical isolates by the microdilution assay. Synergistic or synergistic-to-additive activities were found against all eight isolates by use of both MIC and minimum effective concentration endpoints.

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Al Zyood, Dr Mahmoud M. Al Zyood*,. "Impact of Non-Performing Loans on Saudi Bank Profitability." Indian Journal of Economics and Finance 2, no. 2 (November 30, 2022): 21–24. http://dx.doi.org/10.54105/ijef.d2521.111422.

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Non-performing loans (NPLs) have become increasingly worrying to the Saudi banking sector. Sanctioned loans have a repayment schedule, including principal and interest amounts. Excessive defaults on loans leads to a liquidity crisis throughout the banking sector, and can even cause bank failure. As a result, banks have to cover non-performing loans and maintain reserves under the instructions of the Saudi Arabia Central Bank, which severely affects profitability. This study analyzes the comparative position of non-performing loans in the Saudi banking sector over the period 2009-2017 to determine causes and impacts on bank profitability, using data from annual reports. The study variables are profitability (ROA and ROE) as the dependent variable, and non-performing loans ratio (NPLR) as the independent variable. The data was analyzed by correlation, regression, and analysis of variance (ANOVA) using SPSS. The empirical results represent that NBLR has a negative influence on the dependent variable.

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Barreto, Angela, Joana Santos, Mónica J. B. Amorim, and Vera L. Maria. "Polystyrene Nanoplastics Can Alter the Toxicological Effects of Simvastatin on Danio rerio." Toxics 9, no. 3 (February 26, 2021): 44. http://dx.doi.org/10.3390/toxics9030044.

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Once in the environment, nanoplastics (NPls) may interact with other contaminants, such as pharmaceuticals, potentially acting as carriers and modulating their toxicity. Thus, the main aim of the current study is to investigate how polystyrene (PS) NPls (mean diameter: 60 nm) interact with simvastatin (SIM), an anticholesterolemic drug, and modulate its toxicity to zebrafish (Danio rerio) embryos. PS NPls were carboxyl group functionalized, to promote the interaction/binding of NPls with SIM (worst-case scenarios) and it was fluorescently dyed, allowing to detect the intake. Exposure was 96 h to 0–150 mg/L NPls or 0–150 µg/L SIM, as well as to dual combinations (NPls 0.015 or 1.5 mg/L and SIM 12.5 or 15 µg/L). PS NPls alone did not exert effects whereas SIM (≥ 12.5 µg/L) significantly delayed the hatching, decreased the heartbeat, induced edemas and mortality. The combination of NPls (1.5 mg/L) and SIM (12.5 or 15 µg/L) had significant effects on the survival of the organisms while the correspondent NPls and SIM single exposures did not have significant effects on this endpoint. Concerning the malformations appearance, SIM alone had similar effects than when in co-exposures (0.015 mg/L NPls plus 12.5 or 15 µg/L SIM). Hatching and heartbeat increased after the co-exposures SIM and NPls comparing with SIM single exposures, showing that 0.015 mg/L NPls plus 12.5 or 15 µg/L SIM did not cause significant effects on these endpoints. This study shows that NPls effects on bioavailability and toxicity of other contaminants cannot be ignored when assessing the environmental behavior and risks of NPls.

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Barreto, Angela, Joana Santos, Mónica J. B. Amorim, and Vera L. Maria. "How Can Nanoplastics Affect the Survival, Reproduction, and Behaviour of the Soil Model Enchytraeus crypticus?" Applied Sciences 10, no. 21 (October 30, 2020): 7674. http://dx.doi.org/10.3390/app10217674.

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Nanoplastics (NPls) are ubiquitous in terrestrial environments, with numerous consequences for biodiversity and ecosystems. Research is urgently required to clarify the NPls environmental behaviour, fate and ecotoxicological effects to soil ecosystems. The aim of this research was to assess and comprehend the effects of polystyrene NPls to the terrestrial species Enchytraeus crypticus using survival, reproduction and avoidance behaviour as endpoints. A range of concentrations, 0.015 to 1500 mg NPls/kg LUFA 2.2 (Landwirtschaftliche Untersuchungs- und Forschungsanstalt Speyer, Germany) soil, was tested. Due to the effect of tween 20 and sodium azide (NaN3) on the NPls dispersion, the effects of these compounds were also assessed separately. After 21 d, 1200 and 1500 mg/kg NPls dispersion had significant effects on the organism survival and/or reproduction. However, these effects may be mainly associated with tween 20 and NaN3 present in the NPls dispersion and not with NPls themselves. After 48 h, there was a tendency of the organisms to avoid the NPls spiked soils, being this response significant at 0.015 mg/kg although a reduced avoidance behaviour was observed as NPls concentration increased. The present study provides screening data on the effects of NPls, alone and considering the presence of other compounds like the solvents, which is essential for regulators and strategic management of plastic pollution.

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DeHoratius, C., and P. A. Silver. "Nuclear transport defects and nuclear envelope alterations are associated with mutation of the Saccharomyces cerevisiae NPL4 gene." Molecular Biology of the Cell 7, no. 11 (November 1996): 1835–55. http://dx.doi.org/10.1091/mbc.7.11.1835.

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To identify components involved in nuclear protein import, we used a genetic selection to isolate mutants that mislocalized a nuclear-targeted protein. We identified temperature-sensitive mutants that accumulated several different nuclear proteins in the cytoplasm when shifted to the semipermissive temperature of 30 degrees C; these were termed npl (nuclear protein localization) mutants. We now present the properties of yeast strains bearing mutations in the NPL4 gene and report the cloning of the NPL4 gene and the characterization of the Np14 protein. The npl4-1 mutant was isolated by the previously described selection scheme. The second allele, npl4-2, was identified from an independently derived collection of temperature-sensitive mutants. The npl4-1 and npl4-2 strains accumulate nuclear-targeted proteins in the cytoplasm at the nonpermissive temperature consistent with a defect in nuclear protein import. Using an in vitro nuclear import assay, we show that nuclei prepared from temperature-shifted npl4 mutant cells are unable to import nuclear-targeted proteins, even in the presence of cytosol prepared from wild-type cells. In addition, npl4-2 cells accumulate poly(A)+ RNA in the nucleus at the nonpermissive temperature, consistent with a failure to export mRNA from the nucleus. The npl4-1 and npl4-2 cells also exhibit distinct, temperature-sensitive structural defects: npl4-1 cells project extra nuclear envelope into the cytoplasm, whereas npl4-2 cells from nuclear envelope herniations that appear to be filled with poly(A)+ RNA. The NPL4 gene encodes an essential M(r) 64,000 protein that is located at the nuclear periphery and localizes in a pattern similar to nuclear pore complex proteins. Taken together, these results indicate that this gene encodes a novel nuclear pore complex or nuclear pore complex-associated component required for nuclear membrane integrity and nuclear transport.

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Staresincic, Lidija, Jane Walker, A. Barbara Dirac-Svejstrup, Richard Mitter, and Jesper Q. Svejstrup. "GTP-dependent Binding and Nuclear Transport of RNA Polymerase II by Npa3 Protein." Journal of Biological Chemistry 286, no. 41 (August 15, 2011): 35553–61. http://dx.doi.org/10.1074/jbc.m111.286161.

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We identified XAB1 in a proteomic screen for factors that interact with human RNA polymerase II (RNAPII). Because XAB1 has a conserved Saccharomyces cerevisiae homologue called Npa3, yeast genetics and biochemical analysis were used to dissect the significance of the interaction. Degron-dependent Npa3 depletion resulted in genome-wide transcription decreases, correlating with a loss of RNAPII from genes as measured by chromatin immunoprecipitation. Surprisingly, however, transcription in vitro was unaffected by Npa3, suggesting that it affects a process that is not required for transcription in yeast extracts. Indeed, Npa3 depletion in vivo affects nuclear localization of RNAPII; the polymerase accumulates in the cytoplasm. Npa3 is a member of the GPN-LOOP family of GTPases. Npa3 mutants that either cannot bind GTP or that bind but cannot hydrolyze it are inviable and unable to support nuclear transport of RNAPII. Surprisingly, we were unable to detect interactions between Npa3 and proteins in the classical importin α/β pathway for nuclear import. Interestingly, Npa3-RNAPII binding is significantly increased by the addition of GTP or its slowly hydrolyzable analogue guanosine 5′-3-O-(thio)triphosphate (GTPγS). Moreover, the Npa3 mutant that binds GTP, but cannot hydrolyze it, binds RNAPII even in the absence of added GTP, whereas the mutant that cannot bind GTP is unable to bind the polymerase. Together, our data suggest that Npa3 defines an unconventional pathway for nuclear import of RNAPII, which involves GTP-dependent binding of Npa3 to the polymerase.

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Bredl, Sebastian. "The Role of Non-performing Loans for Bank Lending Rates." Jahrbücher für Nationalökonomie und Statistik 242, no. 2 (December 3, 2021): 223–76. http://dx.doi.org/10.1515/jbnst-2021-0004.

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Abstract Based on bank level data from the euro area, I investigate the role of non-performing loans (NPLs) for lending rates on newly granted loans. The focus is on an effect caused by the stock of NPLs that extends beyond losses that banks have already incorporated into their reported capital positions. The paper assesses the channels through which such an effect occurs. The results indicate that a higher stock of NPLs is associated with higher lending rates. This relation is driven by net NPLs, which constitute the part of NPLs that is not covered by loan loss reserves. Although the stock of NPLs affects banks’ idiosyncratic funding costs as well, the latter do not seem to constitute an important link between the stock of net NPLs and lending behaviour. This is because the relation between idiosyncratic funding costs and lending rates turns out to be rather weak. Furthermore, NPLs do not strongly affect the banks’ interest rate pass-through.

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Pochelon, Alexis, Serge Stoll, and Vera I. Slaveykova. "Polystyrene Nanoplastic Behavior and Toxicity on Crustacean Daphnia magna: Media Composition, Size, and Surface Charge Effects." Environments 8, no. 10 (September 28, 2021): 101. http://dx.doi.org/10.3390/environments8100101.

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Concerns about the possible ecotoxicological implications of nano-sized plastic materials in the freshwater environment are growing with the increasing use of plastic materials. The present study focuses on the behavior and effects of amidine-functionalized polystyrene (NPLs) of 20, 40, 60, and 100-nm-size in freshwaters and different synthetic media. Daphnia magna was exposed to increasing concentrations from 0.5 to 30 mg/L (and from 0.5 to 100 mg/L for 100-nm-sized NPLs). The results revealed no significant aggregation in ultra-pure water, culture media, and synthetic water. In the presence of natural organic matter, NPLs of 20 and 40 nm displayed better stability in both freshwater and synthetic media, whereas a significant aggregation of 60 and 100 nm PS NPLs was found. All the studied PS NPLs with size between 20 and 100 nm exhibited acute toxicity to D. magna. The observed 48-h immobilization strongly depended on the primary size of PS NPLs, with 20 and 40-nm-size PS NPLs inducing a stronger effect in both freshwaters and synthetic media. Water quality variables such as pH, cation and anion composition, and DOC were of secondary importance. The results of the present study confirmed the toxicity of NPLs of different sizes to crustaceans in natural freshwater and synthetic media and demonstrated the importance of the primary size of NPLs in the behavior and effects of NPLs.

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Ozili, Peterson K. "Non-performing loans in European systemic and non-systemic banks." Journal of Financial Economic Policy 12, no. 3 (September 30, 2019): 409–24. http://dx.doi.org/10.1108/jfep-02-2019-0033.

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Purpose The distinction between systemic banks (GSIBs) and non-systemic banks (non-GSIBs) is driven by policy reasons. This study aims to examine the behaviour of non-performing loans in European GSIBs and non-GSIBs from 2004 to 2013. Design/methodology/approach The author uses regression methodology to analyse the association between non-performing loans (NPLs) and the state of the economy. Findings The author finds that more profitable banks witness higher NPLs regardless of them being systemic or non-systemic. Secondly, GSIBs have fewer NPLs during economic booms and during periods of increased lending, while non-GSIBs experience higher NPLs during periods of increased lending. The author also observes that European non-GSIBs that exceed regulatory capital requirement also experience higher NPLs. In the post-crisis period, there is a significant and negative relationship between NPLs and the economic cycle for GSIBs in the post-financial crisis period and a significant and positive relationship between NPLs, loan supply and bank profitability for GSIBs in the post-financial crisis period; on the other hand, there is a significant and negative relationship between NPLs and regulatory capital ratios for non-GSIBs in the post-financial crisis period and a significant and positive relationship between NPLs and bank profitability for non-GSIBs in the post-financial crisis period. The findings have implications. Originality/value To the best of the author’s knowledge, the literature on the determinants of NPL has not empirically examined the behaviour of NPLs in European GSIBs and non-GSIBs. This paper examines this issue to provide insights to help policymakers and academics understand the peculiarities of NPLs in Europe.

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K. Ozili, Peterson, Asma Salman, and Qaisar Ali. "The impact of foreign direct investment inflows on nonperforming loans: the case of UAE." Investment Management and Financial Innovations 17, no. 4 (December 4, 2020): 241–57. http://dx.doi.org/10.21511/imfi.17(4).2020.22.

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The banking sector is at risk of worsening loan quality, which is a major threat to the financial system’s stability. The impact of foreign direct investment (FDI) inflows on nonperforming loans (NPLs) in the United Arab Emirates (UAE) is empirically investigated in this study. The data from 2008 to 2017 are collected and analyzed through the ordinary least squares (OLS) technique. The findings reveal that FDI inflows reduced the size of NPLs during the economic crisis. Also, the combined effect of higher FDI inflows and bank efficiency reduced the size of NPLs for banks, while the combined effect of FDI inflows and better institutions, such as strong regulatory quality, did not reduce the size of NPLs but rather increased the size of NPLs. The findings have implications and contribute to the literature to establish a relationship between FDI inflows and NPLs by examining the relationship between FDI inflows and NPLs in the context of banks in the UAE.

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Abedin, Md Joynal. "Non-Performing Loans and Its Impact on the Banking Sector: An Investigation on the Current Status of Bangladesh." Journal of Asian Development 6, no. 2 (October 26, 2020): 53. http://dx.doi.org/10.5296/jad.v6i2.17874.

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Non-performing loans (NPLs) have become a frustrating issue for the financial institutions in Bangladesh. Our banking industry and the economy in general have taken a negative turn due to the increasing volume of NPLs. This paper aims to investigate the current status of NPLs in the banking industry of Bangladesh. The analysis uses the published data which have been congregated from the annual reports of Bangladesh Bank, websites of the scheduled banks of Bangladesh and the World Bank observed from 2008 to 2019. The study identified that for the last two decades, NPLs are the burning problems for the banks in Bangladesh. Worldwide the standard of NPLs is 2% or less but in our country, it is much intricate. The NPLs percentages in Bangladesh are 4 to 5 times higher than the standard which is disquieting for the entire banking industry. Based on the current investigation, it has been observed that the NPLs ratio is increasing unremittingly with the advancement of time. So, as a financial regulator, the central bank of the country (Bangladesh Bank) must give more emphasize to compactly control the NPLs of the country. This paper contributes by employing new dataset from Bangladesh.

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Ghosh, Amit. "Impact of non-performing loans on US product and labor markets." Journal of Financial Economic Policy 9, no. 3 (August 7, 2017): 302–23. http://dx.doi.org/10.1108/jfep-01-2017-0003.

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Purpose Using time-series data on the US banking industry for the period 1984Q1-2016Q2, the present study aims to examine the impact of both aggregate and sector-specific non-performing loans (NPLs) on aggregate and sectoral product and labor markets. Design/methodology/approach Using both single equation ordinary least squares and instrumental variables regressions, the study compares the sensitivity of sector-specific gross domestic product (GDP) and employment growth to changes in both aggregate and sectoral NPLs. Moreover, the paper uses vector autoregressions (VARs) to dynamically trace the impact and duration of NPLs on different types of real economic activity.. Findings Rise in total NPLs reduces US real GDP growth that is most accentuated for construction sector GDP. Likewise, total NPLs significantly lowers both total and non-farm employment growth, financial activities and construction sector employment growth, with the latter showing most sensitivity. Moreover, NPLs in commercial and industrial sector, consumer lending, non-farm non-residential, construction and land development, single- and multi-family residential sectors reduce corresponding sectoral employment growth. The VARs largely confirm these findings with shocks to total NPLs having the most immediate and persistent inimical impact on construction-sector GDP growth. Practical implications The deleterious impact of different categories of NPLs on both aggregate as well as sector-specific product and labor markets illustrate that a distressed banking sector is a serious obstacle to the real sector. The findings underscore the need not only to clean up NPLs for the sake of banks financial soundness but also to reduce their pernicious effects on the health of the US economy. For bank regulatory authorities in the USA, it indicates constant monitoring of banks in their jurisdiction and identifying early warning signals to mitigate the potential real sector losses due to rising NPLs. Originality value The extant literature on NPLs has mainly focused on explaining its underlying determinants but not on its real sector consequences. The present paper examines the impact of NPLs on different facets of real economic activity, an issue that has been rarely studied and especially not on the US economy. Moreover, the overwhelming majority of existing literature focuses on aggregate NPLs. The relationships derived in such studies, while useful, can mask important differences between different types of NPLs and real economic activity. The present paper explores the impact of disaggregated NPLs in the US banking industry on corresponding sector-specific product and labor markets, again an issue that has not been studied previously.

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Ohshiro, Kazufumi, Prakriti Mudvari, Qing-chang Meng, Suresh K. Rayala, Aysegul A. Sahin, Suzanne A. W. Fuqua, and Rakesh Kumar. "Identification of a Novel Estrogen Receptor-α Variant and Its Upstream Splicing Regulator." Molecular Endocrinology 24, no. 5 (May 1, 2010): 914–22. http://dx.doi.org/10.1210/me.2009-0413.

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Abstract Alternative splicing of precursor mRNA is a fundamental mechanism to generate multiple proteins from a single gene. Although constitutive and alternative mRNA splicing is temporally and spatially regulated, deregulation of mRNA splicing could cause development, progression, and metastasis of tumors. Through yeast two-hybrid screening of a human breast cDNA library using estrogen receptor-α (ERα) as bait, we identified a novel nuclear receptor box containing full-length protein, nuclear protein E3-3 (NPE3-3). Our results revealed that NPE3-3 associates with not only ERα but also with splicing factors, serine/arginine-rich protein (SRp)-30c, SRp40, and splicing factor SC-35, suggesting that NPE3-3 is likely to be involved in regulation of mRNA splicing. Accordingly, transient expression of NPE3-3 in cells resulted in expected splicing of the CD44 control minigene. We also discovered that NPE3-3-overexpressing clones produced a novel, previously unrecognized, alternatively spliced variant of ERα (termed ERαV), which had a molecular size of 37 kDa composed of only exons 1, 2, 7, and 8. ERαV was expressed and sequestered in the cytoplasm in MCF-7 cells stably overexpressing NPE3-3, suggesting its involvement in nongenomic hormone signaling. NPE3-3 clones exhibited up-regulation of ERK1/2 signaling, cyclin D1, and cathepsin D and enhanced tumor cell proliferation, migration, and tumorigenicity. Moreover, direct expression of the ERαV in breast cancer cells stimulated ERK1/2 up-regulation and cyclin D1 expression. We found that ERαV physically interacted with MAPK kinase (MEK)-1/2, and thus, an ERαV and MEK1/2 complex could lead to the activation of the ERK1/2 pathway. Interestingly, NPE3-3 was up-regulated in human breast tumors. These findings revealed a role for NPE3-3 in alternative splicing and suggest that ERα is a physiological target of NPE3-3, leading to a constitutive nongenomic signaling pathway in breast cancer cells.

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Kita, Shunbun, Hitoshi Nishizawa, Yosuke Okuno, Masaki Tanaka, Atsutaka Yasui, Morihiro Matsuda, Yukio Yamada, and Iichiro Shimomura. "Competitive binding of musclin to natriuretic peptide receptor 3 with atrial natriuretic peptide." Journal of Endocrinology 201, no. 2 (February 20, 2009): 287–95. http://dx.doi.org/10.1677/joe-08-0551.

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Musclin is a novel skeletal muscle-derived secretory factor that was isolated by our group. Musclin contains a region homologous to natriuretic peptides (NPs). This study investigated the interaction between musclin and NP receptors (NPRs). Musclin specifically bound to NPR3, but not to NPR1 or NPR2. Musclin and atrial natriuretic peptide (ANP) competed for binding to NPR3. We conducted binding assays using various synthetic musclin peptides and mutant musclin proteins. The first NP-homologous region in musclin (88LDRL91) and the second homologous region (117MDRI120) were responsible cooperatively for high-affinity binding to NPR3. The first NP-homologous region was more importantly associated with binding to NPR3, than the second homologous region. The competitive nature of musclin with ANP for the natriuretic clearance receptor NPR3 was also confirmed in vivo. We conclude that musclin binds to NPR3 competitively with ANP and may affect ANP concentrations in a local or systemic manner.

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Journal articles on the topic 'Npl3'

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