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Journal articles on the topic 'PfpI Family Member Protein'

Author: Grafiati

Published: 6 September 2023

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1

Bankapalli, Kondalarao, SreeDivya Saladi, Sahezeel S. Awadia, Arvind Vittal Goswami, Madhuja Samaddar, and Patrick D'Silva. "Robust Glyoxalase activity of Hsp31, a ThiJ/DJ-1/PfpI Family Member Protein, Is Critical for Oxidative Stress Resistance inSaccharomyces cerevisiae." Journal of Biological Chemistry 290, no. 44 (September 14, 2015): 26491–507. http://dx.doi.org/10.1074/jbc.m115.673624.

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2

Wang, Cunxi, Gregory J. Bean, Chun Ju Chen, Colton R. Kessenich, Jiexin Peng, Nicolo R. Visconti, Jason S. Milligan, et al. "Safety assessment of Mpp75Aa1.1, a new ETX_MTX2 protein from Brevibacillus laterosporus that controls western corn rootworm." PLOS ONE 17, no. 9 (September 8, 2022): e0274204. http://dx.doi.org/10.1371/journal.pone.0274204.

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The recently discovered insecticidal protein Mpp75Aa1.1 from Brevibacillus laterosporus is a member of the ETX_MTX family of beta-pore forming proteins (β-PFPs) expressed in genetically modified (GM) maize to control western corn rootworm (WCR; Diabrotica virgifera virgifera LeConte). In this manuscript, bioinformatic analysis establishes that although Mpp75Aa1.1 shares varying degrees of similarity to members of the ETX_MTX2 protein family, it is unlikely to have any allergenic, toxic, or otherwise adverse biological effects. The safety of Mpp75Aa1.1 is further supported by a weight of evidence approach including evaluation of the history of safe use (HOSU) of ETX_MTX2 proteins and Breviballus laterosporus. Comparisons between purified Mpp75Aa1.1 protein and a poly-histidine-tagged (His-tagged) variant of the Mpp75Aa1.1 protein demonstrate that both forms of the protein are heat labile at temperatures at or above 55°C, degraded by gastrointestinal proteases within 0.5 min, and have no adverse effects in acute mouse oral toxicity studies at a dose level of 1920 or 2120 mg/kg body weight. These results support the use of His-tagged proteins as suitable surrogates for assessing the safety of their non-tagged parent proteins. Taken together, we report that Mpp75Aa1.1 is the first ETX-MTX2 insecticidal protein from B. laterosporus and displays a similar safety profile as typical Cry proteins from Bacillus thuringiensis.

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3

Kouadio, Jean-Louis, Stephen Duff, Michael Aikins, Meiying Zheng, Timothy Rydel, Danqi Chen, Eric Bretsnyder, et al. "Structural and functional characterization of Mpp75Aa1.1, a putative beta-pore forming protein from Brevibacillus laterosporus active against the western corn rootworm." PLOS ONE 16, no. 10 (October 11, 2021): e0258052. http://dx.doi.org/10.1371/journal.pone.0258052.

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The western corn rootworm (WCR), Diabrotica virgifera virgifera LeConte, is a major corn pest of significant economic importance in the United States. The continuous need to control this corn maize pest and the development of field-evolved resistance toward all existing transgenic maize (Zea mays L.) expressing Bacillus thuringiensis (Bt) insecticidal proteins against WCR has prompted the development of new insect-protected crops expressing distinct structural classes of insecticidal proteins. In this current study, we describe the crystal structure and functional characterization of Mpp75Aa1.1, which represents the first corn rootworm (CRW) active insecticidal protein member of the ETX_MTX2 sub-family of beta-pore forming proteins (β-PFPs), and provides new and effective protection against WCR feeding. The Mpp75Aa1.1 crystal structure was solved at 1.94 Å resolution. The Mpp75Aa1.1 is processed at its carboxyl-terminus by WCR midgut proteases, forms an oligomer, and specifically interacts with putative membrane-associated binding partners on the midgut apical microvilli to cause cellular tissue damage resulting in insect death. Alanine substitution of the surface-exposed amino acids W206, Y212, and G217 within the Mpp75Aa1.1 putative receptor binding domain I demonstrates that at least these three amino acids are required for WCR activity. The distinctive spatial arrangement of these amino acids suggests that they are part of a receptor binding epitope, which may be unique to Mpp75Aa1.1 and not present in other ETX_MTX2 proteins that do not have WCR activity. Overall, this work establishes that Mpp75Aa1.1 shares a mode of action consistent with traditional WCR-active Bt proteins despite significant structural differences.

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4

Rodríguez-Rojas, Alexandro, and Jesús Blázquez. "The Pseudomonas aeruginosa pfpI Gene Plays an Antimutator Role and Provides General Stress Protection." Journal of Bacteriology 191, no. 3 (November 21, 2000): 844–50. http://dx.doi.org/10.1128/jb.01081-08.

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ABSTRACT Hypermutator Pseudomonas aeruginosa strains, characterized by an increased spontaneous-mutation rate, are found at high frequencies in chronic lung infections. Hypermutability is associated with the loss of antimutator genes related to DNA repair or damage avoidance systems. Only a few antimutator genes have been described in P. aeruginosa, although there is some evidence that additional genes may be involved in naturally occurring hypermutability. In order to find new P. aeruginosa antimutator genes, we constructed and screened a library of random insertions in the PA14 strain. Some previously described P. aeruginosa and/or Escherichia coli antimutator genes, such as mutS, mutL, uvrD, mutT, ung, and mutY, were detected, indicating a good coverage of our insertional library. One additional mutant contained an insertion in the P. aeruginosa PA14-04650 (pfpI) gene, putatively encoding a member of the DJ-1/ThiJ/PfpI superfamily, which includes chaperones, peptidases, and the Parkinson's disease protein DJ-1a. The pfpI-defective mutants in both PAO1 and PA14 showed higher spontaneous mutation rates than the wild-type strains, suggesting that PfpI plays a key role in DNA protection under nonstress conditions. Moreover, the inactivation of pfpI resulted in a dramatic increase in the H2O2-induced mutant frequency. Global transcription studies showed the induction of bacteriophage Pf1 genes and the repression of genes related to iron metabolism, suggesting that the increased spontaneous-mutant frequency may be due to reduced protection against the basal level of reactive oxygen species. Finally, pfpI mutants are more sensitive to different types of stress and are affected in biofilm formation.

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5

Kim, Hyojung, Aeran Kwon, and Bongjin Lee. "Sturucture of the stress response protein SAV1875 from S. aureus." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C1509. http://dx.doi.org/10.1107/s2053273314084903.

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The DJ-1/ThiJ/PfpI superfamily is a large protein group over diverse organisms, under this superfamily, there are multi-types of proteins such as protease, chaperones, heat shock protein, human parkinson's disease protein. The conserved protein from Staphylococcus aureus SAV1875 is a member of DJ-1 superfamily, but its function is unknown. We have determined the crystal structure of SAV1875 to a resolution of 1.8Å . As expected, the overall fold of the core domain of SAV1875 is similar to that of DJ-1. SAV1875 appears to be a dimer both in solution and the crystal, displaying an oligomerization interface similar to that observed for DJ-1. SAV 1875 contains a possible catalytic triad (Cys105-Glu17-His106) analogous to PfpI, YhbO, and DR1199. The cysteine in this triad (Cys-105) is oxidized in this crystal structure, similar to modifications seen in the cysteine of the DJ-1. This Cys-sulfenic acid is stabilized by hydrogen bonding with Glu17, Gly72, His106. We also have determined the crystal structure of mutated form of reactive Cys, SAV1875 C105D to a resolution of 2.1 Å. Aspartate mutation mimics the the Cys-sulfinic acid, more oxidized form. The aspartate stabilization by hydrogen bonding with neighboring residues are maintained. On the basis of these results, we suggest that SAV1875 might work as a general stress protein involved in the detoxification of the cell from oxygen reactive species.

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6

Zhao, Youfu, Zhonghua Ma, and George W. Sundin. "Comparative Genomic Analysis of the pPT23A Plasmid Family of Pseudomonas syringae." Journal of Bacteriology 187, no. 6 (March 15, 2005): 2113–26. http://dx.doi.org/10.1128/jb.187.6.2113-2126.2005.

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ABSTRACT Members of the pPT23A plasmid family of Pseudomonas syringae play an important role in the interaction of this bacterial pathogen with host plants. Complete sequence analysis of several pPT23A family plasmids (PFPs) has provided a glimpse of the gene content and virulence function of these plasmids. We constructed a macroarray containing 161 genes to estimate and compare the gene contents of 23 newly analyzed and eight known PFPs from 12 pathovars of P. syringae, which belong to four genomospecies. Hybridization results revealed that PFPs could be distinguished by the type IV secretion system (T4SS) encoded and separated into four groups. Twelve PFPs along with pPSR1 from P. syringae pv. syringae, pPh1448B from P. syringae pv. phaseolicola, and pPMA4326A from P. syringae pv. maculicola encoded a type IVA T4SS (VirB-VirD4 conjugative system), whereas 10 PFPs along with pDC3000A and pDC3000B from P. syringae pv. tomato encoded a type IVB T4SS (tra system). Two plasmids encoded both T4SSs, whereas six other plasmids carried none or only a few genes of either the type IVA or type IVB secretion system. Most PFPs hybridized to more than one putative type III secretion system effector gene and to a variety of additional genes encoding known P. syringae virulence factors. The overall gene contents of individual PFPs were more similar among plasmids within each of the four groups based on T4SS genes; however, a number of genes, encoding plasmid-specific functions or hypothetical proteins, were shared among plasmids from different T4SS groups. The only gene shared by all PFPs in this study was the repA gene, which encoded sequences with 87 to 99% amino acid identityamong 25 sequences examined. We proposed a model to illustrate the evolution and gene acquisition of the pPT23A plasmid family. To our knowledge, this is the first such attempt to conduct a global genetic analysis of this important plasmid family.

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7

Portugal, M. E. G., E. M. Souza, F. O. Pedrosa, and E. M. Benelli. "Streptococcus mutans GlnK protein: an unusual PII family member." Brazilian Journal of Medical and Biological Research 44, no. 5 (May 2011): 394–401. http://dx.doi.org/10.1590/s0100-879x2011000500003.

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8

Portugal, M. E. G., E. M. Souza, F. O. Pedrosa, and E. M. Benelli. "Streptococcus mutans GlnK protein: an unusual PII family member." Brazilian Journal of Medical and Biological Research 44, no. 5 (May 2011): 394–401. http://dx.doi.org/10.1590/s0100-879x2011007500042.

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9

Kasof, Gary M., and Bruce C. Gomes. "Livin, a Novel Inhibitor of Apoptosis Protein Family Member." Journal of Biological Chemistry 276, no. 5 (October 9, 2000): 3238–46. http://dx.doi.org/10.1074/jbc.m003670200.

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10

Plano, Gregory V. "Modulation of AraC family member activity by protein ligands." Molecular Microbiology 54, no. 2 (September 14, 2004): 287–90. http://dx.doi.org/10.1111/j.1365-2958.2004.04306.x.

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11

Blake, D. J., R. Nawrotzki, N. Y. Loh, D. C. Gorecki, and K. E. Davies. "-dystrobrevin, a member of the dystrophin-related protein family." Proceedings of the National Academy of Sciences 95, no. 1 (January 6, 1998): 241–46. http://dx.doi.org/10.1073/pnas.95.1.241.

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12

WEINBERG, J., C. WERNECK, and R. MECHAM. "MAGP_1: A novel member of the matricellular protein family." Matrix Biology 25 (November 2006): S19. http://dx.doi.org/10.1016/j.matbio.2006.08.054.

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13

Orosz, Ferenc. "A Fish-specific Member of the TPPP Protein Family?" Journal of Molecular Evolution 75, no. 1-2 (August 2012): 55–72. http://dx.doi.org/10.1007/s00239-012-9521-4.

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14

Cruz, Cristian D., Heidi Palosaari, Jean-Patrick Parisien, Patricia Devaux, Roberto Cattaneo, Toru Ouchi, and Curt M. Horvath. "Measles Virus V Protein Inhibits p53 Family Member p73." Journal of Virology 80, no. 11 (June 1, 2006): 5644–50. http://dx.doi.org/10.1128/jvi.02400-05.

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ABSTRACT Paramyxovirus V proteins function as host interference factors that inactivate antiviral responses, including interferon. Characterization of cellular proteins that copurify with ectopically expressed measles virus V protein has revealed interactions with DNA binding domains of p53 family proteins, p53 and p73. Specific transcriptional assays reveal that expression of measles virus V cDNA inhibits p73, but not p53. Expression of measles virus V cDNA can delay cell death induced by genotoxic stress and also can decrease the abundance of the proapoptotic factor PUMA, a p73 target. Recombinant measles virus with an engineered deficiency in V protein is capable of inducing more severe cytopathic effects than the wild type, implicating measles virus V protein as an inhibitor of cell death. These findings also suggest that p73-PUMA signaling may be a previously unrecognized arm of cellular innate antiviral immunity.

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15

Flower, D. R., A. C. T. North, and T. K. Attwood. "Mouse oncogene protein 24p3 is a member of the Lipocalin protein family." Biochemical and Biophysical Research Communications 180, no. 1 (October 1991): 69–74. http://dx.doi.org/10.1016/s0006-291x(05)81256-2.

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16

Shalaby, Raed, Hector Flores-Romero, and Ana J. García-Sáez. "The Mysteries around the BCL-2 Family Member BOK." Biomolecules 10, no. 12 (December 4, 2020): 1638. http://dx.doi.org/10.3390/biom10121638.

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BOK is an evolutionarily conserved BCL-2 family member that resembles the apoptotic effectors BAK and BAX in sequence and structure. Based on these similarities, BOK has traditionally been classified as a BAX-like pro-apoptotic protein. However, the mechanism of action and cellular functions of BOK remains controversial. While some studies propose that BOK could replace BAK and BAX to elicit apoptosis, others attribute to this protein an indirect way of apoptosis regulation. Adding to the debate, BOK has been associated with a plethora of non-apoptotic functions that makes this protein unpredictable when dictating cell fate. Here, we compile the current knowledge and open questions about this paradoxical protein with a special focus on its structural features as the key aspect to understand BOK biological functions.

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17

Nagpal, Punita, Loni M. Walker, Jeff C. Young, Ami Sonawala, Candace Timpte, Mark Estelle, and Jason W. Reed. "AXR2 Encodes a Member of the Aux/IAA Protein Family." Plant Physiology 123, no. 2 (June 1, 2000): 563–74. http://dx.doi.org/10.1104/pp.123.2.563.

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18

Cheever, A., E. Blackwell, and S. Ceman. "Fragile X protein family member FXR1P is regulated by microRNAs." RNA 16, no. 8 (June 2, 2010): 1530–39. http://dx.doi.org/10.1261/rna.2022210.

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19

Åkerström, Bo, and Lennart Lögdberg. "An intriguing member of the lipocalin protein family: α1-microglobulin." Trends in Biochemical Sciences 15, no. 6 (June 1990): 240–43. http://dx.doi.org/10.1016/0968-0004(90)90037-c.

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20

JONES, P., T. JAKUBOWICZ, F. PITOSSI, F. MAURER, and B. HEMMINGS. "Identification of a new member of the protein kinase family." Cell Biology International Reports 14 (September 1990): 151. http://dx.doi.org/10.1016/0309-1651(90)90706-5.

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21

Minnick, Michael F., Kate N. Sappington, Laura S. Smitherman, Siv G. E. Andersson, Olof Karlberg, and James A. Carroll. "Five-Member Gene Family of Bartonella quintana." Infection and Immunity 71, no. 2 (February 2003): 814–21. http://dx.doi.org/10.1128/iai.71.2.814-821.2003.

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ABSTRACT Bartonella quintana, the agent of trench fever and an etiologic agent of bacillary angiomatosis, has an extraordinarily high hemin requirement for growth compared to other bacterial pathogens. We previously identified the major hemin receptor of the pathogen as a 30-kDa surface protein, termed HbpA. This report describes four additional homologues that share approximately 48% amino acid sequence identity with hbpA. Three of the genes form a paralagous cluster, termed hbpCAB, whereas the other members, hbpD and hbpE, are unlinked. Secondary structure predictions and other evidence suggest that Hbp family members are β-barrels located in the outer membrane and contain eight transmembrane domains plus four extracellular loops. Homologs from a variety of gram-negative pathogens were identified, including Bartonella henselae Pap31, Brucella Omp31, Agrobacterium tumefaciens Omp25, and neisserial opacity proteins (Opa). Family members expressed in vitro-synthesized proteins ranging from ca. 26.5 to 35.1 kDa, with the exception of HbpB, an ∼55.9-kDa protein whose respective gene has been disrupted by a ∼510 GC-rich element containing variable-number tandem repeats. Transcription analysis by quantitative reverse transcriptase-PCR (RT-PCR) indicates that all family members are expressed under normal culture conditions, with hbpD and hbpB transcripts being the most abundant and the rarest, respectively. Mutagenesis of hbpA by allelic exchange produced a strain that exhibited an enhanced hemin-binding phenotype relative to the parental strain, and analysis by quantitative RT-PCR showed elevated transcript levels for the other hbp family members, suggesting that compensatory expression occurs.

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22

Funayama, N., A. Nagafuchi, N. Sato, S. Tsukita, and S. Tsukita. "Radixin is a novel member of the band 4.1 family." Journal of Cell Biology 115, no. 4 (November 15, 1991): 1039–48. http://dx.doi.org/10.1083/jcb.115.4.1039.

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Radixin is an actin barbed-end capping protein which is highly concentrated in the undercoat of the cell-to-cell adherens junction and the cleavage furrow in the interphase and mitotic phase, respectively (Tsukita, Sa., Y. Hieda, and Sh. Tsukita. 1989 a.J. Cell Biol. 108:2369-2382; Sato, N., S. Yonemura, T. Obinata, Sa. Tsukita, and Sh. Tsukita. 1991. J. Cell Biol. 113:321-330). To further understand the structure and functions of the radixin molecule, we isolated and sequenced the cDNA clones encoding mouse radixin. Direct peptide sequencing of radixin and immunological analysis with antiserum to a fusion protein were performed to confirm that the protein encoded by these clones is identical to radixin. The composite cDNA is 4,241 nucleotides long and codes for a 583-amino acid polypeptide with a calculated molecular mass of 68.5 kD. Sequence analysis has demonstrated that mouse radixin shares 75.3% identity with human ezrin, which was reported to be a member of the band 4.1 family. We then isolated the cDNA encoding mouse ezrin. Sequence analysis and Northern blot analysis revealed that radixin and ezrin are similar but distinct (74.9% identity), leading us to conclude that radixin is a novel member of the band 4.1 family. In erythrocytes the band 4.1 protein acts as a key protein in the association of short actin filaments with a plasma membrane protein (glycophorin), together with spectrin. Therefore, the sequence similarity between radixin and band 4.1 protein described in this study favors the idea that radixin plays a crucial role in the association of the barbed ends of actin filaments with the plasma membrane in the cell-to-cell adherens junction and the cleavage furrow.

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23

Kamishikiryo, Jun, Hideo Fukuhara, Yuki Okabe, Kimiko Kuroki, and Katsumi Maenaka. "Molecular Basis for LLT1 Protein Recognition by Human CD161 Protein (NKRP1A/KLRB1)." Journal of Biological Chemistry 286, no. 27 (May 13, 2011): 23823–30. http://dx.doi.org/10.1074/jbc.m110.214254.

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Human Th17 cells express high levels of CD161, a member of the killer cell lectin-like receptor (KLR) family (also referred to as NK receptor-P1A (NKRP1A) or KLRB1), as a representative marker. CD161 is also expressed on natural killer (NK) cells and NKT cells. Lectin-like transcript 1 (LLT1), another KLR family member, was recently identified as a ligand for CD161. This interaction may play pivotal roles in the immunomodulatory functions of Th17 cells as well as those of NK and NKT cells. However, the molecular basis for the interaction is poorly understood. Here we show that the extracellular domain of CD161 bound directly to LLT1 with a Kd of 48 μm and with the fast kinetics typical of cell-cell recognition receptors. Mutagenesis revealed that the similar membrane-distal β-sheet and loop regions of both CD161 and LLT1 were utilized for the binding, and notably, these regions correspond to the ligand-binding sites for major histocompatibility complex (MHC)-recognizing KLRs. Furthermore, we found a pair of detrimental mutations for both molecules that restored the binding. These results reveal a new template model for the recognition mode between the KLR family members and provide insights into the molecular mechanism underlying Th17/NK/NKT-mediated immune responses.

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24

Singh, Mahendra K., Disha Dadke, Emmanuelle Nicolas, Ilya G. Serebriiskii, Sinoula Apostolou, Adrian Canutescu, Brian L. Egleston, and Erica A. Golemis. "A Novel Cas Family Member, HEPL, Regulates FAK and Cell Spreading." Molecular Biology of the Cell 19, no. 4 (April 2008): 1627–36. http://dx.doi.org/10.1091/mbc.e07-09-0953.

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For over a decade, p130Cas/BCAR1, HEF1/NEDD9/Cas-L, and Efs/Sin have defined the Cas (Crk-associated substrate) scaffolding protein family. Cas proteins mediate integrin-dependent signals at focal adhesions, regulating cell invasion and survival; at least one family member, HEF1, regulates mitosis. We here report a previously undescribed novel branch of the Cas protein family, designated HEPL (for HEF1-Efs-p130Cas-like). The HEPL branch is evolutionarily conserved through jawed vertebrates, and HEPL is found in some species lacking other members of the Cas family. The human HEPL mRNA and protein are selectively expressed in specific primary tissues and cancer cell lines, and HEPL maintains Cas family function in localization to focal adhesions, as well as regulation of FAK activity, focal adhesion integrity, and cell spreading. It has recently been demonstrated that upregulation of HEF1 expression marks and induces metastasis, whereas high endogenous levels of p130Cas are associated with poor prognosis in breast cancer, emphasizing the clinical relevance of Cas proteins. Better understanding of the complete protein family should help inform prediction of cancer incidence and prognosis.

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25

Giam, M., T. Okamoto, J. D. Mintern, A. Strasser, and P. Bouillet. "Bcl-2 family member Bcl-G is not a proapoptotic protein." Cell Death & Disease 3, no. 10 (October 2012): e404-e404. http://dx.doi.org/10.1038/cddis.2012.130.

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26

Frankel, Adam, and Steven Clarke. "PRMT3 Is a Distinct Member of the Protein ArginineN-Methyltransferase Family." Journal of Biological Chemistry 275, no. 42 (August 7, 2000): 32974–82. http://dx.doi.org/10.1074/jbc.m006445200.

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27

van den Heuvel, A. P. J. "Binding of protein kinase B to the plakin family member periplakin." Journal of Cell Science 115, no. 20 (October 15, 2002): 3957–66. http://dx.doi.org/10.1242/jcs.00069.

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28

Wang, Yunmei, Chao Fang, Huiyun Gao, Matthew L. Bilodeau, Zijie Zhang, Kevin Croce, Shijian Liu, et al. "Platelet-derived S100 family member myeloid-related protein-14 regulates thrombosis." Journal of Clinical Investigation 124, no. 5 (April 1, 2014): 2160–71. http://dx.doi.org/10.1172/jci70966.

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29

Duan, Run-Shan, Gang-Bin Tang, Hong-Zhen Du, Yi-Wen Hu, Pei-Pei Liu, Ya-Jie Xu, Yu-Qiang Zeng, et al. "Polycomb protein family member CBX7 regulates intrinsic axon growth and regeneration." Cell Death & Differentiation 25, no. 9 (February 19, 2018): 1598–611. http://dx.doi.org/10.1038/s41418-018-0064-0.

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30

Han, Byeong-Gu, Kyung-Chae Jeong, Jea-Won Cho, Byung-Cheon Jeong, Hyun Kyu Song, Jae Young Lee, Dong Hyuk Shin, Sangho Lee, and Byung Il Lee. "Crystal structure ofPyrococcus furiosusPF2050, a member of the DUF2666 protein family." FEBS Letters 586, no. 9 (April 13, 2012): 1384–88. http://dx.doi.org/10.1016/j.febslet.2012.04.004.

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31

Beck, Katy E., Jason G. Kay, and Janice E. A. Braun. "Rdj2, a J protein family member, interacts with cellular prion PrPC." Biochemical and Biophysical Research Communications 346, no. 3 (August 2006): 866–71. http://dx.doi.org/10.1016/j.bbrc.2006.05.185.

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32

Trowbridge, Ian S., Hanne L. Ostergaard, and Pauline Johnson. "CD45: a leukocyte-specific member of the protein tyrosine phosphatase family." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1095, no. 1 (October 1991): 46–56. http://dx.doi.org/10.1016/0167-4889(91)90043-w.

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33

Abe, Mark K., Matthew P. Saelzler, Rafael Espinosa, Kristopher T. Kahle, Marc B. Hershenson, Michelle M. Le Beau, and Marsha Rich Rosner. "ERK8, a New Member of the Mitogen-activated Protein Kinase Family." Journal of Biological Chemistry 277, no. 19 (May 2002): 16733–43. http://dx.doi.org/10.1074/jbc.m112483200.

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34

Melino, G. "Molecular Mechanisms and Function of the p53 Protein Family Member – p73." Biochemistry (Moscow) 85, no. 10 (October 2020): 1202–9. http://dx.doi.org/10.1134/s0006297920100089.

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35

Boase, Natasha Anne, and Sharad Kumar. "NEDD4: The founding member of a family of ubiquitin-protein ligases." Gene 557, no. 2 (February 2015): 113–22. http://dx.doi.org/10.1016/j.gene.2014.12.020.

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36

Iordanova, Janeta V., and Dirk Fasshauer. "Analysis of Scfd2 - A New Member of the SM Protein Family." Biophysical Journal 110, no. 3 (February 2016): 597a. http://dx.doi.org/10.1016/j.bpj.2015.11.3188.

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37

Jialin, Gao, Gu Xuefan, and Zhang Huiwen. "SID1 transmembrane family, member 2 (Sidt2): A novel lysosomal membrane protein." Biochemical and Biophysical Research Communications 402, no. 4 (November 2010): 588–94. http://dx.doi.org/10.1016/j.bbrc.2010.09.133.

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38

Frishman, Dmitrij. "DSBC Protein: A New Member of the Thioredoxin Fold-Containing Family." Biochemical and Biophysical Research Communications 219, no. 3 (February 1996): 686–89. http://dx.doi.org/10.1006/bbrc.1996.0295.

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Lin, Jiing-Huey, Gary Deng, Qihong Huang, and John Morser. "KIAP, a Novel Member of the Inhibitor of Apoptosis Protein Family." Biochemical and Biophysical Research Communications 279, no. 3 (December 2000): 820–31. http://dx.doi.org/10.1006/bbrc.2000.4027.

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Ravanpay, Ali C., and James M. Olson. "E protein dosage influences brain development more than family member identity." Journal of Neuroscience Research 86, no. 7 (2008): 1472–81. http://dx.doi.org/10.1002/jnr.21615.

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Sitasiwi, Agung Janika, Wayan Tunas Artama, Agung Budiyanto, and Edy Dharmana. "Pelacakan Protein Wingless-Type MMTV Integration Site Family Member-4 pada Uterus Mencit (DETECTION WINGLESS-TYPE MMTV INTEGRATION SITE FAMILY MEMBER-4 PROTEIN OF MOUSE UTERUS)." Jurnal Veteriner 17, no. 1 (March 1, 2016): 71–77. http://dx.doi.org/10.19087/jveteriner.2016.17.1.71.

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Żołnierczyk, Jolanta Dominika, and Zofia Maria Kiliańska. "Main Pro-Apoptotic Member of Bcl-2 Family Proteins – Bax." Folia Biologica et Oecologica 6 (December 4, 2010): 5–32. http://dx.doi.org/10.2478/v10107-009-0004-3.

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Programmed cell death (apoptosis) plays a vital role in the regulation of cellular homeostasis. Because of apoptosis fundamental importance, this process is highly regulated. One important set of factors involved in apoptosis regulation is the Bcl-2 family proteins. Bcl-2 family members form a complex regulatory network that controls cell survival and death in response to different physiological and pathological signals. This family includes both pro- and anti-apoptotic members, and Bax protein (Mol wt 21 kDa) is a major pro-apoptotic factor with multifunctional activity. This review summarizes new data about the main representative of Bcl-2 family – Bax, its structure and mechanism(s) by which this protein modulates apoptosis.

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Wu, Di, Jan J. Vonk, Felix Salles, Danara Vonk, Martin Haslbeck, Ronald Melki, Steven Bergink, and Harm H. Kampinga. "The N terminus of the small heat shock protein HSPB7 drives its polyQ aggregation–suppressing activity." Journal of Biological Chemistry 294, no. 25 (May 16, 2019): 9985–94. http://dx.doi.org/10.1074/jbc.ra118.007117.

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Heat shock protein family B (small) member 7 (HSPB7) is a unique, relatively unexplored member within the family of human small heat shock proteins (HSPBs). Unlike most HSPB family members, HSPB7 does not oligomerize and so far has not been shown to associate with any other member of the HSPB family. Intriguingly, it was found to be the most potent member within the HSPB family to prevent aggregation of proteins with expanded polyglutamine (polyQ) stretches. How HSPB7 suppresses polyQ aggregation has remained elusive so far. Here, using several experimental strategies, including in vitro aggregation assay, immunoblotting and fluorescence approaches, we show that the polyQ aggregation-inhibiting activity of HSPB7 is fully dependent on its flexible N-terminal domain (NTD). We observed that the NTD of HSPB7 is both required for association with and inhibition of polyQ aggregation. Remarkably, replacing the NTD of HSPB1, which itself cannot suppress polyQ aggregation, with the NTD of HSPB7 resulted in a hybrid protein that gained anti-polyQ aggregation activity. The hybrid NTDHSPB7–HSPB1 protein displayed a reduction in oligomer size and, unlike WT HSPB1, associated with polyQ. However, experiments with phospho-mimicking HSPB1 mutants revealed that de-oligomerization of HSPB1 alone does not suffice to gain polyQ aggregation–inhibiting activity. Together, our results reveal that the NTD of HSPB7 is both necessary and sufficient to bind to and suppress the aggregation of polyQ-containing proteins.

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Umeda, Rie, Tomohiro Nishizawa, and Osamu Nureki. "Crystallization of the human tetraspanin protein CD9." Acta Crystallographica Section F Structural Biology Communications 75, no. 4 (April 1, 2019): 254–59. http://dx.doi.org/10.1107/s2053230x1801840x.

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The tetraspanin family of proteins with four membrane-spanning proteins function in a wide range of physiological processes in higher organisms, including cell migration and proliferation, cell fusion, fertilization and virus infection. Although the recently reported structure of CD81 unveiled the basic architecture of this family for the first time, further structural and functional studies are required in order to understand the mechanistic details of the complicated functions of the tetraspanin-family proteins. In this study, attempts were made to crystallize human CD9, a representative member of the tetraspanin family, and it was demonstrated that the truncation of a variable region in the second long extracellular loop significantly improved crystal growth.

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Taura, T., H. Krebber, and P. A. Silver. "A member of the Ran-binding protein family, Yrb2p, is involved in nuclear protein export." Proceedings of the National Academy of Sciences 95, no. 13 (June 23, 1998): 7427–32. http://dx.doi.org/10.1073/pnas.95.13.7427.

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Wilhelmsen, Kevin, Sandy H. M. Litjens, Ingrid Kuikman, Ntambua Tshimbalanga, Hans Janssen, Iman van den Bout, Karine Raymond, and Arnoud Sonnenberg. "Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin." Journal of Cell Biology 171, no. 5 (December 5, 2005): 799–810. http://dx.doi.org/10.1083/jcb.200506083.

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Despite their importance in cell biology, the mechanisms that maintain the nucleus in its proper position in the cell are not well understood. This is primarily the result of an incomplete knowledge of the proteins in the outer nuclear membrane (ONM) that are able to associate with the different cytoskeletal systems. Two related ONM proteins, nuclear envelope spectrin repeat (nesprin)–1 and –2, are known to make direct connections with the actin cytoskeleton through their NH2-terminal actin-binding domain (ABD). We have now isolated a third member of the nesprin family that lacks an ABD and instead binds to the plakin family member plectin, which can associate with the intermediate filament (IF) system. Overexpression of nesprin-3 results in a dramatic recruitment of plectin to the nuclear perimeter, which is where these two molecules are colocalized with both keratin-6 and -14. Importantly, plectin binds to the integrin α6β4 at the cell surface and to nesprin-3 at the ONM in keratinocytes, suggesting that there is a continuous connection between the nucleus and the extracellular matrix through the IF cytoskeleton.

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Manna, Pulak R., Matthew T. Dyson, Darrell W. Eubank, Barbara J. Clark, Enzo Lalli, Paolo Sassone-Corsi, Anthony J. Zeleznik, and Douglas M. Stocco. "Regulation of Steroidogenesis and the Steroidogenic Acute Regulatory Protein by a Member of the cAMP Response-Element Binding Protein Family." Molecular Endocrinology 16, no. 1 (January 1, 2002): 184–99. http://dx.doi.org/10.1210/mend.16.1.0759.

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Abstract The mitochondrial phosphoprotein, the steroidogenic acute regulatory (StAR) protein, is an essential component in the regulation of steroid biosynthesis in adrenal and gonadal cells through cAMP-dependent pathways. In many cases transcriptional induction by cAMP is mediated through the interaction of a cAMP response-element binding protein (CREB) family member with a consensus cAMP response element (CRE; 5′-TGACGTCA-3′) found in the promoter of target genes. The present investigation was carried out to determine whether a CRE-binding protein (CREB) family member [CREB/CRE modulator (CREM) family] was involved in the regulation of steroidogenesis and StAR protein expression. Transient expression of wild- type CREB in MA-10 mouse Leydig tumor cells further increased the levels of (Bu)2cAMP-induced progesterone synthesis, StAR promoter activity, StAR mRNA, and StAR protein. These responses were significantly inhibited by transfection with a dominant-negative CREB (A-CREB), or with a CREB mutant that cannot be phosphorylated (CREB-M1), the latter observation indicating the importance of phosphorylation of a CREB/CREM family member in steroidogenesis and StAR expression. The CREB/CREM-responsive region in the mouse StAR gene was located between −110 and −67 bp upstream of the transcriptional start site. An oligonucleotide probe (−96/−67 bp) containing three putative half-sites for 5′-canonical CRE sequences (TGAC) demonstrated the formation of protein-DNA complexes in EMSAs with recombinant CREB protein as well as with nuclear extracts from MA-10 or Y-1 mouse adrenal tumor cells. The predominant binding factor observed with EMSA was found to be the CREM protein as demonstrated using specific antibodies and RT-PCR analyses. The CRE elements identified within the− 96/−67 bp region were tested for cAMP responsiveness by generating mutations in each of the CRE half-sites either alone or in combination. Although each of the CRE sites contribute in part to the CREM response, the CRE2 appears to be the most important site as determined by EMSA and by reporter gene analyses. Binding specificity was further assessed using specific antibodies to CREB/CREM family members, cold competitors, and mutations in the target sites that resulted in either supershift and/or inhibition of these complexes. We also demonstrate that the inducible cAMP early repressor markedly diminished the endogenous effects of CREM on cAMP-induced StAR promoter activity and on StAR mRNA expression. These are the first observations to provide evidence for the functional involvement of a CREB/CREM family member in the acute regulation of trophic hormone-stimulated steroidogenesis and StAR gene expression.

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Leulliot, Nicolas, Sophie Quevillon-Cheruel, Marc Graille, Marc Schiltz, Karine Blondeau, Joël Janin, and Herman Van Tilbeurgh. "Crystal structure of yeast YER010Cp, aknotable member of the RraA protein family." Protein Science 14, no. 10 (October 2005): 2751–58. http://dx.doi.org/10.1110/ps.051684005.

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Gras, S., B. Fernandez, V. Chaumont, P. Carpentier, J. Armengaud, and D. Housset. "Structure of a PACE protein: PAB0955, first member of new GTPase family." Acta Crystallographica Section A Foundations of Crystallography 61, a1 (August 23, 2005): c498. http://dx.doi.org/10.1107/s0108767305079468.

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Auble, David T., and Susanne M. Steggerda. "Testing for DNA Tracking by MOT1, a SNF2/SWI2 Protein Family Member." Molecular and Cellular Biology 19, no. 1 (January 1, 1999): 412–23. http://dx.doi.org/10.1128/mcb.19.1.412.

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ABSTRACT Proteins in the SNF2/SWI2 family use ATP hydrolysis to catalyze rearrangements in diverse protein-DNA complexes. How ATP hydrolysis is coupled to these rearrangements is unknown, however. One attractive model is that these ATPases are ATP-dependent DNA-tracking enzymes. This idea was tested for the SNF2/SWI2 protein family member MOT1. MOT1 is an essential Saccharomyces cerevisiae transcription factor that uses ATP to dissociate TATA binding protein (TBP) from DNA. By using a series of DNA templates with one or two TATA boxes in combination with binding sites for heterologous DNA binding “roadblock” proteins, the ability of MOT1 to track along DNA was assayed. The results demonstrate that, following ATP-dependent TBP-DNA dissociation, MOT1 dissociates rapidly from the DNA by a mechanism that does not require a DNA end. Template commitment footprinting experiments support the conclusion that ATP-dependent DNA tracking by MOT1 does not occur. These results support a model in which MOT1 drives TBP-DNA dissociation by a mechanism that involves a transient, ATP-dependent interaction with TBP-DNA which does not involve ATP-dependent DNA tracking.

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