Journal articles: 'Proteins maturation'

1

Hellen, Christopher U. T., and Eckard Wimmer. "Maturation of poliovirus capsid proteins." Virology 187, no. 2 (April 1992): 391–97. http://dx.doi.org/10.1016/0042-6822(92)90440-z.

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Garoff, Henrik, Roger Hewson, and Dirk-Jan E. Opstelten. "Virus Maturation by Budding." Microbiology and Molecular Biology Reviews 62, no. 4 (December 1, 1998): 1171–90. http://dx.doi.org/10.1128/mmbr.62.4.1171-1190.1998.

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SUMMARY Enveloped viruses mature by budding at cellular membranes. It has been generally thought that this process is driven by interactions between the viral transmembrane proteins and the internal virion components (core, capsid, or nucleocapsid). This model was particularly applicable to alphaviruses, which require both spike proteins and a nucleocapsid for budding. However, genetic studies have clearly shown that the retrovirus core protein, i.e., the Gag protein, is able to form enveloped particles by itself. Also, budding of negative-strand RNA viruses (rhabdoviruses, orthomyxoviruses, and paramyxoviruses) seems to be accomplished mainly by internal components, most probably the matrix protein, since the spike proteins are not absolutely required for budding of these viruses either. In contrast, budding of coronavirus particles can occur in the absence of the nucleocapsid and appears to require two membrane proteins only. Biochemical and structural data suggest that the proteins, which play a key role in budding, drive this process by forming a three-dimensional (cage-like) protein lattice at the surface of or within the membrane. Similarly, recent electron microscopic studies revealed that the alphavirus spike proteins are also engaged in extensive lateral interactions, forming a dense protein shell at the outer surface of the viral envelope. On the basis of these data, we propose that the budding of enveloped viruses in general is governed by lateral interactions between peripheral or integral membrane proteins. This new concept also provides answers to the question of how viral and cellular membrane proteins are sorted during budding. In addition, it has implications for the mechanism by which the virion is uncoated during virus entry.

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Remington, S. James. "Fluorescent proteins: maturation, photochemistry and photophysics." Current Opinion in Structural Biology 16, no. 6 (December 2006): 714–21. http://dx.doi.org/10.1016/j.sbi.2006.10.001.

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Matthews, Glenn. "Introduction: Proteolytic maturation of secretory proteins." Seminars in Cell & Developmental Biology 9, no. 1 (February 1998): 1–2. http://dx.doi.org/10.1006/scdb.1997.0193.

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Sumi, Mamta P., and Arnab Ghosh. "Hsp90 in Human Diseases: Molecular Mechanisms to Therapeutic Approaches." Cells 11, no. 6 (March 12, 2022): 976. http://dx.doi.org/10.3390/cells11060976.

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The maturation of hemeprotein dictates that they incorporate heme and become active, but knowledge of this essential cellular process remains incomplete. Studies on chaperon Hsp90 has revealed that it drives functional heme maturation of inducible nitric oxide synthase (iNOS), soluble guanylate cyclase (sGC) hemoglobin (Hb) and myoglobin (Mb) along with other proteins including GAPDH, while globin heme maturations also need an active sGC. In all these cases, Hsp90 interacts with the heme-free or apo-protein and then drives the heme maturation by an ATP dependent process before dissociating from the heme-replete proteins, suggesting that it is a key player in such heme-insertion processes. As the studies on globin maturation also need an active sGC, it connects the globin maturation to the NO-sGC (Nitric oxide-sGC) signal pathway, thereby constituting a novel NO-sGC-Globin axis. Since many aggressive cancer cells make Hbβ/Mb to survive, the dependence of the globin maturation of cancer cells places the NO-sGC signal pathway in a new light for therapeutic intervention. Given the ATPase function of Hsp90 in heme-maturation of client hemeproteins, Hsp90 inhibitors often cause serious side effects and this can encourage the alternate use of sGC activators/stimulators in combination with specific Hsp90 inhibitors for better therapeutic intervention.

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Gross, I. "Regulation of fetal lung maturation." American Journal of Physiology-Lung Cellular and Molecular Physiology 259, no. 6 (December 1, 1990): L337—L344. http://dx.doi.org/10.1152/ajplung.1990.259.6.l337.

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The recent identification of the genes for the surfactant proteins has greatly facilitated the study of the regulation of fetal lung alveolar epithelial cell development at the molecular level. In general, expression of the genes for the surfactant proteins is enhanced by the same hormones that stimulate phospholipid synthesis. There are, however, some notable differences that indicate that the genes for the different components of surfactant are independently regulated. Species differences in the response of the surfactant proteins to hormones such as glucocorticoids and adenosine 3',5'-cyclic monophosphate have also been demonstrated. This review focuses on current knowledge of the hormonal regulation of the surfactant proteins against a background of previous studies of lung development.

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Davis, Brandi N., Aaron C. Hilyard, Giorgio Lagna, and Akiko Hata. "SMAD proteins control DROSHA-mediated microRNA maturation." Nature 454, no. 7200 (June 11, 2008): 56–61. http://dx.doi.org/10.1038/nature07086.

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PAGES, Jean Marie, and Claude LAZDUNSKI. "Maturation of Exported Proteins in Escherichia coli." European Journal of Biochemistry 124, no. 3 (March 3, 2005): 561–66. http://dx.doi.org/10.1111/j.1432-1033.1982.tb06630.x.

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Long, Courtney L., William L. Berry, Ying Zhao, Xiao-Hong Sun, and Mary Beth Humphrey. "E proteins regulate osteoclast maturation and survival." Journal of Bone and Mineral Research 27, no. 12 (November 19, 2012): 2476–89. http://dx.doi.org/10.1002/jbmr.1707.

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Abaturov, A. E., and V. L. Babуch. "MiRNA biogenesis. Part 1. Maturation of pre-miRNA. Maturation of canonical miRNAs." CHILD`S HEALTH 16, no. 2 (May 13, 2021): 200–207. http://dx.doi.org/10.22141/2224-0551.16.2.2021.229886.

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The scientific review presents the biogenesis of miRNAs. To write the article, information was searched using databases Scopus, Web of Science, MedLine, PubMed, Google Scholar, EMBASE, Global Health, The Cochrane Library, CyberLeninka. The article presents a brief description of the RNA sequence encoding miRNAs. It is emphasized that microRNAs, depending on the location of the sequence encoding them in the genome, are divided into two major groups: canonical and non-canonical miRNAs. It has been found that a single locus of a sequence encoding a miRNA can generate a series of non-coding mature transcripts. It is noted that there are canonical and non-canonical (alternative) ways of maturation of pri-miRNAs. The canonical path of maturation of miRNAs results from the functioning of DROSHA and DICER proteins. Intranuclear processing of pri-miRNA by the DROSHA protein is revealed, which leads to the formation of pre-miRNAs transported from the cell nucleus to the cytoplasm, where under the influence of the DICER protein they are converted into duplex microRNAs. Duplex miRNAs are recruited by Argonaute (AGO) proteins, on which they are spun, and as a result one of the two strands of RNA becomes mature miRNA. Non-canonical primary miRNA transcripts can be subjected to DROSHA-, DGCR8-independent, and DICER-independent processing. The dysfunction of microprocessor proteins and nuclear export of pre-miRNAs is accompanied by the development of some human diseases. Thus, in the biogenesis of miRNAs, there are canonical and non-canonical (alternative) ways of maturation of pri-miRNAs. The canonical path of maturation of primary microRNA transcripts is due to the functioning of DROSHA and DICER proteins. The non-canonical path of maturation of pre-miRNAs is performed by DROSHA-, DGCR8-independent, and DICER-independent processing. The dysfunction of various mechanisms of the canonical path of maturation of pre-miRNA is associated with the development of some human diseases.

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Watanabe, Satoshi, Daisuke Sasaki, Taiga Tominaga, and Kunio Miki. "Structural basis of [NiFe] hydrogenase maturation by Hyp proteins." Biological Chemistry 393, no. 10 (October 1, 2012): 1089–100. http://dx.doi.org/10.1515/hsz-2012-0197.

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Abstract [NiFe] hydrogenases catalyze reversible hydrogen production/consumption. The active site of [NiFe] hydrogenases contains a complex NiFe(CN)2CO center, and the biosynthesis/maturation of these enzymes is a complex and dynamic process, primarily involving six Hyp proteins (HypABCDEF). HypA and HypB are involved in the Ni insertion, whereas the other four Hyp proteins (HypCDEF) are required for the biosynthesis, assembly and insertion of the Fe(CN)2CO group. Over the last decades, a large number of functional and structural studies on maturation proteins have been performed, revealing detailed functions of each Hyp protein and the framework of the maturation pathway. This article will focus on recent advances in structural studies of the Hyp proteins and on mechanistic insights into the [NiFe] hydrogenase maturation.

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Roland, Mélanie, Jonathan Przybyla-Toscano, Florence Vignols, Nathalie Berger, Tamanna Azam, Loick Christ, Véronique Santoni, et al. "The plastidial Arabidopsis thaliana NFU1 protein binds and delivers [4Fe-4S] clusters to specific client proteins." Journal of Biological Chemistry 295, no. 6 (January 6, 2020): 1727–42. http://dx.doi.org/10.1074/jbc.ra119.011034.

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Proteins incorporating iron–sulfur (Fe-S) co-factors are required for a plethora of metabolic processes. Their maturation depends on three Fe-S cluster assembly machineries in plants, located in the cytosol, mitochondria, and chloroplasts. After de novo formation on scaffold proteins, transfer proteins load Fe-S clusters onto client proteins. Among the plastidial representatives of these transfer proteins, NFU2 and NFU3 are required for the maturation of the [4Fe-4S] clusters present in photosystem I subunits, acting upstream of the high-chlorophyll fluorescence 101 (HCF101) protein. NFU2 is also required for the maturation of the [2Fe-2S]-containing dihydroxyacid dehydratase, important for branched-chain amino acid synthesis. Here, we report that recombinant Arabidopsis thaliana NFU1 assembles one [4Fe-4S] cluster per homodimer. Performing co-immunoprecipitation experiments and assessing physical interactions of NFU1 with many [4Fe-4S]-containing plastidial proteins in binary yeast two-hybrid assays, we also gained insights into the specificity of NFU1 for the maturation of chloroplastic Fe-S proteins. Using bimolecular fluorescence complementation and in vitro Fe-S cluster transfer experiments, we confirmed interactions with two proteins involved in isoprenoid and thiamine biosynthesis, 1-hydroxy-2-methyl-2-(E)-butenyl-4-diphosphate synthase and 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase, respectively. An additional interaction detected with the scaffold protein SUFD enabled us to build a model in which NFU1 receives its Fe-S cluster from the SUFBC2D scaffold complex and serves in the maturation of specific [4Fe-4S] client proteins. The identification of the NFU1 partner proteins reported here more clearly defines the role of NFU1 in Fe-S client protein maturation in Arabidopsis chloroplasts among other SUF components.

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Sadeghi, Hamid M., Giulio Innamorati, and Mariel Birnbaumer. "Maturation of Receptor Proteins in Eukaryotic Expression Systems." Journal of Receptors and Signal Transduction 17, no. 1-3 (January 1997): 433–45. http://dx.doi.org/10.3109/10799899709036619.

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UCHIDA, Takeshi. "Structure and Function of Cytochrome c Maturation Proteins." Seibutsu Butsuri 47, no. 2 (2007): 112–17. http://dx.doi.org/10.2142/biophys.47.112.

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Spangler, S. A., and C. C. Hoogenraad. "Liprin-α proteins: scaffold molecules for synapse maturation." Biochemical Society Transactions 35, no. 5 (October 25, 2007): 1278–82. http://dx.doi.org/10.1042/bst0351278.

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Synapses are specialized communication junctions between neurons whose plasticity provides the structural and functional basis for information processing and storage in the brain. Recent biochemical, genetic and imaging studies in diverse model systems are beginning to reveal the molecular mechanisms by which synaptic vesicles, ion channels, receptors and other synaptic components assemble to make a functional synapse. Recent evidence has shown that the formation and function of synapses are critically regulated by the liprin-α family of scaffolding proteins. The liprin-αs have been implicated in pre- and post-synaptic development by recruiting synaptic proteins and regulating synaptic cargo transport. Here, we will summarize the diversity of liprin binding partners, highlight the factors that control the function of liprin-αs at the synapse and discuss how liprin-α family proteins regulate synapse formation and synaptic transmission.

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Kramer, Günter, Ayala Shiber, and Bernd Bukau. "Mechanisms of Cotranslational Maturation of Newly Synthesized Proteins." Annual Review of Biochemistry 88, no. 1 (June 20, 2019): 337–64. http://dx.doi.org/10.1146/annurev-biochem-013118-111717.

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The timely production of functional proteins is of critical importance for the biological activity of cells. To reach the functional state, newly synthesized polypeptides have to become enzymatically processed, folded, and assembled into oligomeric complexes and, for noncytosolic proteins, translocated across membranes. Key activities of these processes occur cotranslationally, assisted by a network of machineries that transiently engage nascent polypeptides at distinct phases of translation. The sequence of events is tuned by intrinsic features of the nascent polypeptides and timely association of factors with the translating ribosome. Considering the dynamics of translation, the heterogeneity of cellular proteins, and the diversity of interaction partners, it is a major cellular achievement that these processes are temporally and spatially so precisely coordinated, minimizing the generation of damaged proteins. This review summarizes the current progress we have made toward a comprehensive understanding of the cotranslational interactions of nascent chains, which pave the way to their functional state.

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Blackman, Sheila A., Scott H. Wettlaufer, Ralph L. Obendorf, and A. Carl Leopold. "Maturation Proteins Associated with Desiccation Tolerance in Soybean." Plant Physiology 96, no. 3 (July 1, 1991): 868–74. http://dx.doi.org/10.1104/pp.96.3.868.

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Netz, Daili J. A., Judita Mascarenhas, Oliver Stehling, Antonio J. Pierik, and Roland Lill. "Maturation of cytosolic and nuclear iron–sulfur proteins." Trends in Cell Biology 24, no. 5 (May 2014): 303–12. http://dx.doi.org/10.1016/j.tcb.2013.11.005.

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Rawe, V. Y., A. J. Espanñol, F. Nodar, and S. Brugo Olmedo. "Mammalian Oocyte Maturation and Microtubule-Associated Proteins Dynamics." Fertility and Sterility 84 (September 2005): S143. http://dx.doi.org/10.1016/j.fertnstert.2005.07.349.

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Kirchhoff, C., C. Osterhoff, I. Pera, and S. Schröter. "Function of human epididymal proteins in sperm maturation." Andrologia 30, no. 4-5 (April 24, 2009): 225–32. http://dx.doi.org/10.1111/j.1439-0272.1998.tb01164.x.

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Sipos, Katalin, Heike Lange, Zsuzsanna Fekete, Pascaline Ullmann, Roland Lill, and Gyula Kispal. "Maturation of Cytosolic Iron-Sulfur Proteins Requires Glutathione." Journal of Biological Chemistry 277, no. 30 (May 14, 2002): 26944–49. http://dx.doi.org/10.1074/jbc.m200677200.

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Deretic, V., Laura E. Via, Rutilio A. Fratti, and Dusanka Deretic. "Mycobacterial phagosome maturation, rab proteins, and intracellular trafficking." Electrophoresis 18, no. 14 (1997): 2542–47. http://dx.doi.org/10.1002/elps.1150181409.

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Dacheux, Jean-Louis, Jean Luc Gatti, and Françoise Dacheux. "Contribution of epididymal secretory proteins for spermatozoa maturation." Microscopy Research and Technique 61, no. 1 (May 1, 2003): 7–17. http://dx.doi.org/10.1002/jemt.10312.

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Gegenfurtner, Katrin, Florian Flenkenthaler, Thomas Fröhlich, Eckhard Wolf, and Georg J. Arnold. "The impact of transcription inhibition during in vitro maturation on the proteome of bovine oocytes†." Biology of Reproduction 103, no. 5 (August 28, 2020): 1000–1011. http://dx.doi.org/10.1093/biolre/ioaa149.

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Abstract Proper oocyte maturation is a prerequisite for successful reproduction and requires the resumption of meiosis to the metaphase II stage (MII). In bovine oocytes, nuclear maturation has been shown to occur in in vitro maturing cumulus-enclosed oocytes (COCs) in the absence of transcription, but their developmental capacity is reduced compared to transcriptionally competent COCs. To assess the impact of transcription during in vitro maturation of bovine COCs on the quantitative oocyte proteome, a holistic nano-LC–MS/MS analysis of germinal vesicle oocytes and MII oocytes matured with or without addition of the transcription inhibitor actinomycin D (ActD) was carried out. Analyzing eight biological replicates for each of the three groups, a total of 2018 proteins was identified. These could be clearly classified into proteins depending or not depending on transcription during oocyte maturation. Proteins whose abundance increased after maturation irrespective of transcription inhibition - and hence independent of transcription - were related to the cell cycle, reflecting the progression of meiosis, and to cellular component organization, which is crucial for cytoplasmic maturation. In contrast, transcription-dependent proteins were associated with cell–cell adhesion and translation. Since a high rate of protein synthesis in oocytes has been shown to correlate with their developmental competence, oocyte maturation in transcriptionally impaired COCs is apparently disturbed. Our experiments reveal that impaired transcription during in vitro maturation of COCs has a substantial effect on specific components of the oocyte proteome, and that transcription is required for specific classes of oocyte proteins predominantly involved in translation.

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Stevens-Hernandez, Christian J., and Lesley J. Bruce. "Reticulocyte Maturation." Membranes 12, no. 3 (March 10, 2022): 311. http://dx.doi.org/10.3390/membranes12030311.

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Changes to the membrane proteins and rearrangement of the cytoskeleton must occur for a reticulocyte to mature into a red blood cell (RBC). Different mechanisms of reticulocyte maturation have been proposed to reduce the size and volume of the reticulocyte plasma membrane and to eliminate residual organelles. Lysosomal protein degradation, exosome release, autophagy and the extrusion of large autophagic–endocytic hybrid vesicles have been shown to contribute to reticulocyte maturation. These processes may occur simultaneously or perhaps sequentially. Reticulocyte maturation is incompletely understood and requires further investigation. RBCs with membrane defects or cation leak disorders caused by genetic variants offer an insight into reticulocyte maturation as they present characteristics of incomplete maturation. In this review, we compare the structure of the mature RBC membrane with that of the reticulocyte. We discuss the mechanisms of reticulocyte maturation with a focus on incomplete reticulocyte maturation in red cell variants.

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Smirnov, Alexandre. "Research Progress in RNA-Binding Proteins." International Journal of Molecular Sciences 24, no. 1 (December 21, 2022): 58. http://dx.doi.org/10.3390/ijms24010058.

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RNA-binding proteins are everywhere and accompany RNA molecules at every stage of their molecular life, from “birth” (transcription) through “growing up” (maturation), “active life” (molecular function) until “death” (turnover) [...]

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Ge, Peng, and Z. Hong Zhou. "Chaperone fusion proteins aid entropy-driven maturation of class II viral fusion proteins." Trends in Microbiology 22, no. 2 (February 2014): 100–106. http://dx.doi.org/10.1016/j.tim.2013.11.006.

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Yen, Benjamin C., and Christopher F. Basler. "Effects of Filovirus Interferon Antagonists on Responses of Human Monocyte-Derived Dendritic Cells to RNA Virus Infection." Journal of Virology 90, no. 10 (March 9, 2016): 5108–18. http://dx.doi.org/10.1128/jvi.00191-16.

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ABSTRACTDendritic cells (DCs) are major targets of filovirus infectionin vivo. Previous studies have shown that the filoviruses Ebola virus (EBOV) and Marburg virus (MARV) suppress DC maturationin vitro. Both viruses also encode innate immune evasion functions. The EBOV VP35 (eVP35) and the MARV VP35 (mVP35) proteins each can block RIG-I-like receptor signaling and alpha/beta interferon (IFN-α/β) production. The EBOV VP24 (eVP24) and MARV VP40 (mVP40) proteins each inhibit the production of IFN-stimulated genes (ISGs) by blocking Jak-STAT signaling; however, this occurs by different mechanisms, with eVP24 blocking nuclear import of tyrosine-phosphorylated STAT1 and mVP40 blocking Jak1 function. MARV VP24 (mVP24) has been demonstrated to modulate host cell antioxidant responses. Previous studies demonstrated that eVP35 is sufficient to strongly impair primary human monocyte-derived DC (MDDC) responses upon stimulation induced through the RIG-I-like receptor pathways. We demonstrate that mVP35, like eVP35, suppresses not only IFN-α/β production but also proinflammatory responses after stimulation of MDDCs with RIG-I activators. In contrast, eVP24 and mVP40, despite suppressing ISG production upon RIG-I activation, failed to block upregulation of maturation markers or T cell activation. mVP24, although able to stimulate expression of antioxidant response genes, had no measurable impact of DC function. These data are consistent with a model where filoviral VP35 proteins are the major suppressors of DC maturation during filovirus infection, whereas the filoviral VP24 proteins and mVP40 are insufficient to prevent DC maturation.IMPORTANCEThe ability to suppress the function of dendritic cells (DCs) likely contributes to the pathogenesis of disease caused by the filoviruses Ebola virus and Marburg virus. To clarify the basis for this DC suppression, we assessed the effect of filovirus proteins known to antagonize innate immune signaling pathways, including Ebola virus VP35 and VP24 and Marburg virus VP35, VP40, and VP24, on DC maturation and function. The data demonstrate that the VP35s from Ebola virus and Marburg virus are the major suppressors of DC maturation and that the effects on DCs of the remaining innate immune inhibitors are minor.

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Lu, Rebecca, and David G. Drubin. "Selection and stabilization of endocytic sites by Ede1, a yeast functional homologue of human Eps15." Molecular Biology of the Cell 28, no. 5 (March 2017): 567–75. http://dx.doi.org/10.1091/mbc.e16-06-0391.

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During clathrin-mediated endocytosis (CME), endocytic-site maturation can be divided into two stages corresponding to the arrival of the early and late proteins at the plasma membrane. The early proteins are required to capture cargo and position the late machinery, which includes proteins involved in actin assembly and membrane scission. However, the mechanism by which early-arriving proteins select and stabilize endocytic sites is not known. Ede1, one of the earliest proteins recruited to endocytic sites, facilitates site initiation and stabilization. Deletion of EDE1 results in fewer CME initiations and defects in the timing of vesicle maturation. Here we made truncation mutants of Ede1 to better understand how different domains contribute to its recruitment to CME sites, site selection, and site maturation. We found that the minimal domains required for efficient Ede1 localization at CME sites are the third EH domain, the proline-rich region, and the coiled-coil region. We also found that many strains expressing ede1 truncations could support a normal rate of site initiation but still had defects in site-maturation timing, indicating separation of Ede1 functions. When expressed in yeast, human Eps15 localized to the plasma membrane, where it recruited late-phase CME proteins and supported productive endocytosis, identifying it as an Ede1 functional homologue.

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Yang, Huijun, Weijing Liu, Shen Song, Lina Bai, Yu Nie, Yongping Bai, and Guogang Zhang. "Proteogenomics Integrating Reveal a Complex Network, Alternative Splicing, Hub Genes Regulating Heart Maturation." Genes 13, no. 2 (January 28, 2022): 250. http://dx.doi.org/10.3390/genes13020250.

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Heart maturation is an essentially biological process for neonatal heart transition to adult heart, thus illustrating the mechanism of heart maturation may be helpful to explore postnatal heart development and cardiac cardiomyopathy. This study combined proteomic analysis based on isobaric tags for relative and absolute quantitation (iTRAQ) and transcriptome analysis based on RNA sequencing to detect the proteins and genes associated with heart maturation in mice. The proteogenomics integrating analysis identified 254 genes/proteins as commonly differentially expressed between neonatal and adult hearts. Functional and pathway analysis demonstrated that these identified genes/proteins contribute to heart maturation mainly by regulating mRNA processing and energy metabolism. Genome-wide alternative splicing (AS) analysis showed that some important sarcomere and energy-associated genes undergo different AS events. Through the Cytoscape plug-in CytoHubba, a total of 23 hub genes were found and further confirmed by RT-qPCR. Next, we verified that the most up-regulated hub gene, Ogdhl, plays an essential role in heart maturation by detecting energy metabolism phenotype changes in the Ogdhl-interfering cardiomyocytes. Together, we revealed a complex gene network, AS genes and patterns, and candidate hub genes controlling heart maturation by proteome and transcriptome combination analysis.

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Frank-Vaillant, Marie, Catherine Jessus, René Ozon, James L. Maller, and Olivier Haccard. "Two Distinct Mechanisms Control the Accumulation of Cyclin B1 and Mos inXenopusOocytes in Response to Progesterone." Molecular Biology of the Cell 10, no. 10 (October 1999): 3279–88. http://dx.doi.org/10.1091/mbc.10.10.3279.

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Progesterone-induced meiotic maturation of Xenopusoocytes requires the synthesis of new proteins, such as Mos and cyclin B. Synthesis of Mos is thought to be necessary and sufficient for meiotic maturation; however, it has recently been proposed that newly synthesized proteins binding to p34cdc2could be involved in a signaling pathway that triggers the activation of maturation-promoting factor. We focused our attention on cyclin B proteins because they are synthesized in response to progesterone, they bind to p34cdc2, and their microinjection into resting oocytes induces meiotic maturation. We investigated cyclin B accumulation in response to progesterone in the absence of maturation-promoting factor–induced feedback. We report here that the cdk inhibitor p21cip1, when microinjected into immatureXenopus oocytes, blocks germinal vesicle breakdown induced by progesterone, by maturation-promoting factor transfer, or by injection of okadaic acid. After microinjection of p21cip1, progesterone fails to induce the activation of MAPK or p34cdc2, and Mos does not accumulate. In contrast, the level of cyclin B1 increases normally in a manner dependent on down-regulation of cAMP-dependent protein kinase but independent of cap-ribose methylation of mRNA.

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Johnstone, RM, and K. Teng. "Membrane Remodelling During Reticulocyte Maturation." Physiology 4, no. 1 (February 1, 1989): 37–42. http://dx.doi.org/10.1152/physiologyonline.1989.4.1.37.

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During maturation, reticulocytes lose many membrane functions, including the transferrin receptor. Immunocytochemical studies reveal that after endocytosis the transferrin receptor (and many other membrane proteins) is packaged into multivesicular bodies. The vesicular contents are externalized by exocytosis. The specificity of such membrane processing underlies the changing properties of the cells' surfaces.

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Wright, J. T., and W. T. Butler. "Alteration of Enamel Proteins in Hypomaturation Amelogenesis Imperfecta." Journal of Dental Research 68, no. 9 (September 1989): 1328–30. http://dx.doi.org/10.1177/00220345890680090801.

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Amelogenesis imperfecta (AI) is a diverse group of disorders that affects primarily the enamel of teeth through a number of developmental processes. The purpose of this study was to characterize the enamel proteins in normal enamel and in hypomaturation AI enamel. Impacted teeth, which were at similar stages of development, were obtained for analysis from an individual with Al and from normal healthy controls. Evaluation of the amino acid profile and quantity of organic material collected showed that there was an excess of enamel protein material that had an amelogenin-like amino acid profile in mature hypomaturation AI enamel. The AI enamel protein content was 5%, while the control enamel had 0.1% protein (by weight). These findings indicate that the maturation process had been altered in this type of AI, and that maturation did not progress beyond the initial stages of secondary mineralization. Since this disorder is inherited as an autosomal recessive condition, it seems likely that the primary defect involves an abnormality in the mechanism for protein removal in enamel maturation.

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Gillam, Shirley. "Molecular biology of rubella virus structural proteins." Biochemistry and Cell Biology 72, no. 9-10 (September 1, 1994): 349–56. http://dx.doi.org/10.1139/o94-048.

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Rubella virus is a small, enveloped, positive-stranded RNA virus in the Togaviridae family and bears similarities to the prototype alphaviruses in terms of its genome organization and strategy for viral gene expression. Despite being an important human pathogen, the cell biology of rubella virus remains poorly characterized. This review focuses on the molecular biology of rubella virus structural proteins, with emphasis on the proteolytic processing and maturation of virus structural proteins, the glycosylation requirement for intracellular transport and function of glycoproteins, and the localization of hemagglutinin- and virus-neutralizing epitopes. A number of significant differences between rubella virus and alphavirus structural protein expression and maturation were discovered.Key words: rubella virus, N-linked glycosylation, epitope mapping, proteolytic processing.

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Kim, Jumi, Ji-Su Kim, Young-Joo Jeon, Dong-Wook Kim, Tae-Ho Yang, Yunjo Soh, Hak Lee, et al. "Identification of maturation and protein synthesis related proteins from porcine oocytes during in vitro maturation." Proteome Science 9, no. 1 (2011): 28. http://dx.doi.org/10.1186/1477-5956-9-28.

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Cemma, Marija, Sergio Grinstein, and John H. Brumell. "Autophagy proteins are not universally required for phagosome maturation." Autophagy 12, no. 9 (July 8, 2016): 1440–46. http://dx.doi.org/10.1080/15548627.2016.1191724.

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Turner, Raymond J., Andriyka L. Papish, and Frank Sargent. "Sequence analysis of bacterial redox enzyme maturation proteins (REMPs)." Canadian Journal of Microbiology 50, no. 4 (April 1, 2004): 225–38. http://dx.doi.org/10.1139/w03-117.

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The twin-arginine protein transport (Tat) system is a remarkable molecular machine dedicated to the translocation of fully folded proteins across energy-transducing membranes. Complex cofactor-containing Tat substrates acquire their cofactors prior to export, and substrate proteins actually require to be folded before transport can proceed. Thus, it is very likely that mechanisms exist to prevent wasteful export of immature Tat substrates or to curb competition between immature and mature substrates for the transporter. Here we assess the primary sequence relationships between the accessory proteins implicated in this process during assembly of key respiratory enzymes in the model prokaryote Escherichia coli. For each respiratory enzyme studied, a redox enzyme maturation protein (REMP) was assigned. The main finding from this review was the hitherto unexpected link between the Tat-linked REMP DmsD and the nitrate reductase biosynthetic protein NarJ. The evolutionary link between Tat transport and cofactor insertion processes is discussed.Key words: Tat translocase, twin-arginine leader, hydrogenase, nitrate reductase, TMAO reductase, DMSO reductase, formate dehydrogenase, Tor, Dms, Hya, Hyb, Fdh, Nap.

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Lelouard, Hugues, Evelina Gatti, Fanny Cappello, Olivia Gresser, Voahirana Camosseto, and Philippe Pierre. "Transient aggregation of ubiquitinated proteins during dendritic cell maturation." Nature 417, no. 6885 (May 2002): 177–82. http://dx.doi.org/10.1038/417177a.

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Hara-Nishimura, Ikuko, Tomoo Shimada, Nagako Hiraiwa, and Mikio Nishimura. "Vacuolar Processing Enzyme Responsible for Maturation of Seed Proteins." Journal of Plant Physiology 145, no. 5-6 (March 1995): 632–40. http://dx.doi.org/10.1016/s0176-1617(11)81275-7.

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Przybyla-Toscano, Jonathan, Mélanie Roland, Frédéric Gaymard, Jérémy Couturier, and Nicolas Rouhier. "Roles and maturation of iron–sulfur proteins in plastids." JBIC Journal of Biological Inorganic Chemistry 23, no. 4 (January 18, 2018): 545–66. http://dx.doi.org/10.1007/s00775-018-1532-1.

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Wang, Qinchuan. "Xin proteins and intercalated disc maturation, signaling and diseases." Frontiers in Bioscience 17, no. 7 (2012): 2566. http://dx.doi.org/10.2741/4072.

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Hausen, Peter, Ya Hui Wang, Christine Dreyer, Reimer Stick, Ursula Müller, and Metta Riebesell. "Distribution of nuclear proteins during maturation of the Xenopus oocyte." Development 89, Supplement (November 1, 1985): 17–34. http://dx.doi.org/10.1242/dev.89.supplement.17.

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The internal structure of the Xenopus oocyte is reorganized during the hormone-induced egg maturation. A cytological survey of the intracellular movements and changes is described. The behaviour of the nuclear lamina protein and of three nucleoplasmic proteins during these processes was studied by immunocytology. The proteins are finally deposited in the egg in different patterns brought about by their differential behaviour during the process of maturation.

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Nim, Yap Shing, and Kam-Bo Wong. "The Maturation Pathway of Nickel Urease." Inorganics 7, no. 7 (July 6, 2019): 85. http://dx.doi.org/10.3390/inorganics7070085.

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Maturation of urease involves post-translational insertion of nickel ions to form an active site with a carbamylated lysine ligand and is assisted by urease accessory proteins UreD, UreE, UreF and UreG. Here, we review our current understandings on how these urease accessory proteins facilitate the urease maturation. The urease maturation pathway involves the transfer of Ni2+ from UreE → UreG → UreF/UreD → urease. To avoid the release of the toxic metal to the cytoplasm, Ni2+ is transferred from one urease accessory protein to another through specific protein–protein interactions. One central theme depicts the role of guanosine triphosphate (GTP) binding/hydrolysis in regulating the binding/release of nickel ions and the formation of the protein complexes. The urease and [NiFe]-hydrogenase maturation pathways cross-talk with each other as UreE receives Ni2+ from hydrogenase maturation factor HypA. Finally, the druggability of the urease maturation pathway is reviewed.

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Hube, Michaela, Melanie Blokesch, and August Böck. "Network of Hydrogenase Maturation in Escherichia coli: Role of Accessory Proteins HypA and HybF." Journal of Bacteriology 184, no. 14 (July 15, 2002): 3879–85. http://dx.doi.org/10.1128/jb.184.14.3879-3885.2002.

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ABSTRACT We have studied the roles of the auxiliary protein HypA and of its homolog HybF in hydrogenase maturation. A mutation in hypA leads to the nearly complete blockade of maturation solely of hydrogenase 3 whereas a lesion in hybF drastically but not totally reduces maturation and activity of isoenzymes 1 and 2. The residual level of matured enzymes in the hybF mutant was shown to be due to the function of HypA; HybF, conversely, was responsible for a minimal residual activity of hydrogenase 3 in the mutant hypA strain. Accordingly, a hypA ΔhybF double mutant was completely blocked in the maturation process. However, the inclusion of high nickel concentrations in the medium could restore limited activity of all three hydrogenases. The results of this study and of previous work (M. Blokesch, A. Magalon, and A. Böck, J. Bacteriol. 189:2817-2822, 2001) show that the maturation of the three functional hydrogenases from Escherichia coli is intimately connected via the activity of proteins HypA and HypC and of their homologs HybF and HybG, respectively. The results also support the suggestion of Olson et al. (J. W. Olson, N. S. Mehta, and R. J. Maier, Mol. Microbiol. 39:176-182, 2001) that HypA cooperates with HypB in the insertion of nickel into the precursor of the large hydrogenase subunit. Whereas HypA is predominantly involved in the maturation of hydrogenase 3, HybF takes over its function in the maturation of isoenzymes 1 and 2.

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Bhojwani, M., M. Marx, F. Melo-Sterza, W. Kanitz, C. Leiding, and W. Tomek. "307CHARACTERIZATION OF PROTEIN PHOSPHORYLATIONS IN THE COURSE OF MEIOTIC MATURATION OF BOVINE OOCYTES." Reproduction, Fertility and Development 16, no. 2 (2004): 273. http://dx.doi.org/10.1071/rdv16n1ab307.

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The importance of protein phosphorylations during meiotic maturation (transition from prophase I to metaphase II) of oocytes is documented by the fact that the inhibition of the M-phase kinases, cdc2k or MAPK, arrests the oocytes in the GV stage. A detailed knowledge of the targets of these kinases during this stage of development is still missing. Therefore, we have analyzed the proteome of bovine oocytes by high resolution 2D-gel electrophoresis to detect differences in the expression and phosphorylation state of proteins in the course of in vitro maturation (IVM). Bovine oocytes were matured for different times in TCM 199 containing 3% BSA and 300 oocytes each in GV stage (0-h maturation), in GVBD/M I (10-h maturation) or in M II stage (240h maturation) were separated on the gels. The proteins were visualized by staining them with silver or with the fluorescence dye Sypro Ruby, and phosphorylated proteins were detected by Western Blotting with Ser-, Thr-, or Tyr-phosphorylation specific antibodies or by staining with the phosphoprotein specific fluorescence dye Pro-Q Diamond. Gels made from oocytes at the above mentioned maturation stages were compared by a computerized gel-overlay software program (2D Decodon, Greitswald, Germany). The overall protein synthesis was statistically analysed by ANOVA (SigmaStat, Ekrath, Germany), pairwise multiple comparison procedure. Only distinct spots with a difference greater than 30% in their optical densities were considered to be differently expressed or phosphorylated. The results showed a three-fold increase in the rate of overall protein synthesis (p 0.05) during GVBD. Newly synthesized proteins were detected mainly in the higher molecular weight (MW) range (60–80kDa), and protein degradations were found mainly in the lower MW range (20–40kDa) after GVBD. Preliminary data obtained by analyzing the phosphorylation pattern showed that obviously no phosphorylated proteins could be detected in the GV-stage oocytes. Phosphorylation of different proteins was observed at the time of GVBD after 6 to 10h IVM, concomitantly with the activation of cdc2k and MAPK. A maximum of phosphorylated proteins was observed in metaphase II. The first results obtained by performing peptide mass fingerprinting using MALDI-Tof showed that members of the family of heat-shock proteins, ribosomal proteins and putative zinc finger proteins (transcription regulators) were differently expressed or phosphorylated during IVM. This work was supported by the DFG, To 178/1-1, 2 and by the Eibl-Stiftung.

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Schultz, A., and A. Rein. "Maturation of murine leukemia virus env proteins in the absence of other viral proteins." Virology 145, no. 2 (September 1985): 335–39. http://dx.doi.org/10.1016/0042-6822(85)90168-0.

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Liu, Jing, Xinhua Guo, Narla Mohandas, Joel A. Chasis, and Xiuli An. "Membrane remodeling during reticulocyte maturation." Blood 115, no. 10 (March 11, 2010): 2021–27. http://dx.doi.org/10.1182/blood-2009-08-241182.

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Abstract The transition of reticulocytes into erythrocytes is accompanied by extensive changes in the structure and properties of the plasma membrane. These changes include an increase in shear resistance, loss of surface area, and acquisition of a biconcave shape. The processes by which these changes are effected have remained largely undefined. Here we examine how the expression of 30 distinct membrane proteins and their interactions change during murine reticulocyte maturation. We show that tubulin and cytosolic actin are lost, whereas the membrane content of myosin, tropomyosin, intercellular adhesion molecule-4, glucose transporter-4, Na-K-ATPase, sodium/hydrogen exchanger 1, glycophorin A, CD47, Duffy, and Kell is reduced. The degradation of tubulin and actin is, at least in part, through the ubiquitin-proteasome degradation pathway. In regard to the protein-protein interactions, the formation of membrane-associated spectrin tetramers from dimers is unperturbed, whereas the interactions responsible for the formation of the membrane-skeletal junctions are weaker in reticulocytes, as is the attachment of transmembrane proteins to these structures. This weakness, in part, results from the elevated phosphorylation of 4.1R in reticulocytes, which leads to a decrease in shear resistance by reducing its interaction with spectrin and actin. These observations begin to unravel the mechanistic basis of crucial changes accompanying reticulocyte maturation.

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Desjardins, M., N. N. Nzala, R. Corsini, and C. Rondeau. "Maturation of phagosomes is accompanied by changes in their fusion properties and size-selective acquisition of solute materials from endosomes." Journal of Cell Science 110, no. 18 (September 15, 1997): 2303–14. http://dx.doi.org/10.1242/jcs.110.18.2303.

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Maturation of phagosomes is characterized by changes in their polypeptides, phosphorylated proteins and phospholipid composition. Kinetic analyses have shown that a variety of proteins associate and dissociate from latex-containing phagosomes at precise intervals during phagolysosome biogenesis. In an attempt to link these temporal biochemical modifications to functional changes, we have examined the in vivo fusion properties of aging endosomes and phagosomes. Using an in vivo fusion assay at the electron microscope, we measured the rate of exchange of bovine serum albumin-gold (5 and 16 nm particles) between endosomes and latex-bead-containing phagosomes. The results obtained indicate that the maturation of phagosomes is accompanied by changes of their fusion properties. Early phagosomes were shown to fuse preferentially with early endocytic organelles and to gradually acquire the ability to fuse with late endocytic organelles. Furthermore, the transfer of bovine serum albumin-gold from endosomes to phagosomes is size-dependent, a process also modulated by the maturation of these organelles, in agreement with the concept that transient fusion events occur between endosomes and phagosomes. Biochemical analysis showed variations in the levels of rab proteins associated with phagosomes during maturation while other ‘fusion’ proteins, including synaptobrevin1 and synaptobrevin2, remained constant.

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Dasgupta, Anindya, and Duncan W. Wilson. "ATP Depletion Blocks Herpes Simplex Virus DNA Packaging and Capsid Maturation." Journal of Virology 73, no. 3 (March 1, 1999): 2006–15. http://dx.doi.org/10.1128/jvi.73.3.2006-2015.1999.

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ABSTRACT During herpes simplex virus (HSV) assembly, immature procapsids must expel their internal scaffold proteins, transform their outer shell to form mature polyhedrons, and become packaged with the viral double-stranded (ds) DNA genome. A large number of virally encoded proteins are required for successful completion of these events, but their molecular roles are poorly understood. By analogy with the dsDNA bacteriophage we reasoned that HSV DNA packaging might be an ATP-requiring process and tested this hypothesis by adding an ATP depletion cocktail to cells accumulating unpackaged procapsids due to the presence of a temperature-sensitive lesion in the HSV maturational protease UL26. Following return to permissive temperature, HSV capsids were found to be unable to package DNA, suggesting that this process is indeed ATP dependent. Surprisingly, however, the display of epitopes indicative of capsid maturation was also inhibited. We conclude that either formation of these epitopes directly requires ATP or capsid maturation is normally arrested by a proofreading mechanism until DNA packaging has been successfully completed.

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Gerber, Jana, Karina Neumann, Corinna Prohl, Ulrich Mühlenhoff, and Roland Lill. "The Yeast Scaffold Proteins Isu1p and Isu2p Are Required inside Mitochondria for Maturation of Cytosolic Fe/S Proteins." Molecular and Cellular Biology 24, no. 11 (June 1, 2004): 4848–57. http://dx.doi.org/10.1128/mcb.24.11.4848-4857.2004.

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ABSTRACT Iron-sulfur (Fe/S) proteins are located in mitochondria, cytosol, and nucleus. Mitochondrial Fe/S proteins are matured by the iron-sulfur cluster (ISC) assembly machinery. Little is known about the formation of Fe/S proteins in the cytosol and nucleus. A function of mitochondria in cytosolic Fe/S protein maturation has been noted, but small amounts of some ISC components have been detected outside mitochondria. Here, we studied the highly conserved yeast proteins Isu1p and Isu2p, which provide a scaffold for Fe/S cluster synthesis. We asked whether the Isu proteins are needed for biosynthesis of cytosolic Fe/S clusters and in which subcellular compartment the Isu proteins are required. The Isu proteins were found to be essential for de novo biosynthesis of both mitochondrial and cytosolic Fe/S proteins. Several lines of evidence indicate that Isu1p and Isu2p have to be located inside mitochondria in order to perform their function in cytosolic Fe/S protein maturation. We were unable to mislocalize Isu1p to the cytosol due to the presence of multiple, independent mitochondrial targeting signals in this protein. Further, the bacterial homologue IscU and the human Isu proteins (partially) complemented the defects of yeast Isu protein-depleted cells in growth rate, Fe/S protein biogenesis, and iron homeostasis, yet only after targeting to mitochondria. Together, our data suggest that the Isu proteins need to be localized in mitochondria to fulfill their functional requirement in Fe/S protein maturation in the cytosol.

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Journal articles on the topic 'Proteins maturation'

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