RPT5

Summary

Gene Symbol: RPT5
Description: proteasome regulatory particle base subunit RPT5
Alias: YTA1, proteasome regulatory particle base subunit RPT5
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. Glickman M, Rubin D, Fried V, Finley D. The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol Cell Biol. 1998;18:3149-62 pubmed
    ..Overall, regulatory particles from yeasts and mammals are remarkably similar, suggesting that the specific mechanistic features of the proteasome have been closely conserved over the course of evolution. ..
  2. Rubin D, Glickman M, Larsen C, Dhruvakumar S, Finley D. Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome. EMBO J. 1998;17:4909-19 pubmed
    ..In summary, ATP promotes protein breakdown by the proteasome through multiple mechanisms, as reflected by the diverse phenotypes of the rpt mutants. ..
  3. Le Tallec B, Barrault M, Guerois R, Carré T, Peyroche A. Hsm3/S5b participates in the assembly pathway of the 19S regulatory particle of the proteasome. Mol Cell. 2009;33:389-99 pubmed publisher
    ..Finally, we identify the putative species-specific 19S subunit S5b as a functional homolog of the Hsm3 chaperone in mammals. These findings shed light on chaperone-assisted proteasome assembly in eukaryotes. ..
  4. Saeki Y, Toh e A, Yokosawa H. Rapid isolation and characterization of the yeast proteasome regulatory complex. Biochem Biophys Res Commun. 2000;273:509-15 pubmed
    ..In contrast with the previously reported result showing that Rpn10, a multiubiquitin chain binding subunit, is a component of the base complex, we present evidence that the lid complex isolated from wild-type yeast contains Rpn10. ..
  5. Funakoshi M, Tomko R, Kobayashi H, Hochstrasser M. Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base. Cell. 2009;137:887-99 pubmed publisher
    ..Nas2 forms a complex with the Rpt4 and Rpt5 ATPases and enhances 26S proteasome formation in vivo and in vitro...
  6. Park S, Roelofs J, Kim W, Robert J, Schmidt M, Gygi S, et al. Hexameric assembly of the proteasomal ATPases is templated through their C termini. Nature. 2009;459:866-70 pubmed publisher
    ..Our studies show that assembly of the proteasome base is a rapid yet highly orchestrated process. ..
  7. Lander G, Estrin E, Matyskiela M, Bashore C, Nogales E, Martin A. Complete subunit architecture of the proteasome regulatory particle. Nature. 2012;482:186-91 pubmed publisher
    ..We provide a structural basis for the ability of the proteasome to degrade a diverse set of substrates and thus regulate vital cellular processes. ..
  8. Sone T, Saeki Y, Toh e A, Yokosawa H. Sem1p is a novel subunit of the 26 S proteasome from Saccharomyces cerevisiae. J Biol Chem. 2004;279:28807-16 pubmed
    ..The results suggest that Sem1, possibly hDSS1, is a novel subunit of the 26 S proteasome and plays a role in ubiquitin-dependent proteolysis. ..
  9. Matyskiela M, Lander G, Martin A. Conformational switching of the 26S proteasome enables substrate degradation. Nat Struct Mol Biol. 2013;20:781-8 pubmed publisher
    ..Notably, Rpn11 moves from an occluded position to directly above the central pore, thus facilitating substrate deubiquitination concomitant with translocation. ..

More Information

Publications39

  1. Tomko R, Funakoshi M, Schneider K, Wang J, Hochstrasser M. Heterohexameric ring arrangement of the eukaryotic proteasomal ATPases: implications for proteasome structure and assembly. Mol Cell. 2010;38:393-403 pubmed publisher
    ..disulfide engineering to show that the eukaryotic ATPases form a ring with the arrangement Rpt1-Rpt2-Rpt6-Rpt3-Rpt4-Rpt5 in fully assembled proteasomes. The arrangement is consistent with known assembly intermediates...
  2. Wang X, Yen J, Kaiser P, Huang L. Regulation of the 26S proteasome complex during oxidative stress. Sci Signal. 2010;3:ra88 pubmed publisher
  3. Ng W, Sergeyenko T, Zeng N, Brown J, Römisch K. Characterization of the proteasome interaction with the Sec61 channel in the endoplasmic reticulum. J Cell Sci. 2007;120:682-91 pubmed
    ..Mutations in the ATP-binding sites of individual Rpt proteins all reduced the affinity of 19S complexes for the ER, suggesting that the 19S base in the ATP-bound conformation docks at the Sec61 channel. ..
  4. Saeki Y, Isono E, Toh e A. Preparation of ubiquitinated substrates by the PY motif-insertion method for monitoring 26S proteasome activity. Methods Enzymol. 2005;399:215-27 pubmed
    ..In this communication, we describe that Sic1 was successfully ubiquitinated by the PY motif-insertion method and demonstrate that Sic1 thus ubiquitinated was degraded by the purified yeast 26S proteasome. ..
  5. Funakoshi M, Hochstrasser M. Small epitope-linker modules for PCR-based C-terminal tagging in Saccharomyces cerevisiae. Yeast. 2009;26:185-92 pubmed publisher
    ..The set of plasmids has been deposited in the non-profit plasmid repository Addgene (http://www.addgene.org). ..
  6. Luan B, Huang X, Wu J, Mei Z, Wang Y, Xue X, et al. Structure of an endogenous yeast 26S proteasome reveals two major conformational states. Proc Natl Acad Sci U S A. 2016;113:2642-7 pubmed publisher
    ..Structure-guided biochemical analysis reveals enhanced deubiquitylating enzyme activity of Rpn11 upon assembly of the lid. Our structures serve as a molecular basis for mechanistic understanding of proteasome function. ..
  7. Gonzalez F, Delahodde A, Kodadek T, Johnston S. Recruitment of a 19S proteasome subcomplex to an activated promoter. Science. 2002;296:548-50 pubmed
    ..These data indicate that in vivo, the base of the 19S complex functions independently of the larger complex and plays a direct, nonproteolytic role in RNA polymerase II transcription. ..
  8. Seong K, Baek J, Ahn B, Yu M, Kim J. Rpn10p is a receptor for ubiquitinated Gcn4p in proteasomal proteolysis. Mol Cells. 2007;24:194-9 pubmed
    ..These results suggest that Rpn10p is the receptor that binds the polyubiquitin chain during ubiquitin-dependent proteolysis of Gcn4p. ..
  9. Pietroni P, Vasisht N, Cook J, Roberts D, Lord J, Hartmann Petersen R, et al. The proteasome cap RPT5/Rpt5p subunit prevents aggregation of unfolded ricin A chain. Biochem J. 2013;453:435-45 pubmed publisher
    ..degraded, but the mammalian 26S proteasome AAA (ATPase associated with various cellular activities)-ATPase subunit RPT5 acts as a chaperone that prevents aggregation of denatured RTA and stimulates recovery of catalytic RTA activity in..
  10. Li Y, Yan J, Kim I, Liu C, Huo K, Rao H. Rad4 regulates protein turnover at a postubiquitylation step. Mol Biol Cell. 2010;21:177-85 pubmed publisher
    ..Our findings will help to unravel the detailed mechanisms underlying the roles of Rad23 and Rad4 in proteolysis and also the interplay between DNA repair and proteolysis. ..
  11. Bohovych I, Kastora S, Christianson S, Topil D, Kim H, Fangman T, et al. Oma1 Links Mitochondrial Protein Quality Control and TOR Signaling To Modulate Physiological Plasticity and Cellular Stress Responses. Mol Cell Biol. 2016;36:2300-12 pubmed publisher
  12. Bashore C, Dambacher C, Goodall E, Matyskiela M, Lander G, Martin A. Ubp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome. Nat Struct Mol Biol. 2015;22:712-9 pubmed publisher
    ..Ubp6 may thus act as a ubiquitin-dependent 'timer' to coordinate individual processing steps at the proteasome and modulate substrate degradation. ..
  13. Barrault M, Richet N, Godard C, Murciano B, Le Tallec B, Rousseau E, et al. Dual functions of the Hsm3 protein in chaperoning and scaffolding regulatory particle subunits during the proteasome assembly. Proc Natl Acad Sci U S A. 2012;109:E1001-10 pubmed publisher
    ..In addition, we provide structural and biochemical evidence on how Hsm3/S5b may regulate the 19S RP association to the 20S CP proteasome. Our data point out the diverse functions of assembly chaperones. ..
  14. Wrobel L, Topf U, Bragoszewski P, Wiese S, Sztolsztener M, Oeljeklaus S, et al. Mistargeted mitochondrial proteins activate a proteostatic response in the cytosol. Nature. 2015;524:485-8 pubmed publisher
    ..UPRam provides a means for buffering the consequences of physiological slowdown in mitochondrial protein import and for counteracting pathologies that are caused or contributed by mitochondrial dysfunction. ..
  15. Lee S, De La Mota Peynado A, Roelofs J. Loss of Rpt5 protein interactions with the core particle and Nas2 protein causes the formation of faulty proteasomes that are inhibited by Ecm29 protein. J Biol Chem. 2011;286:36641-51 pubmed publisher
    ..One of these chaperones, Nas2/p27, binds to the C-terminal region of the AAA-ATPase Rpt5. We report here that the tail of Rpt5 provides two functions...
  16. Ding Z, Fu Z, Xu C, Wang Y, Wang Y, Li J, et al. High-resolution cryo-EM structure of the proteasome in complex with ADP-AlFx. Cell Res. 2017;27:373-385 pubmed publisher
    ..Our results provide new insights into the mechanisms of nucleotide-driven allosteric cooperativity of the complex and of the substrate processing by the proteasome. ..
  17. Saeki Y, Sone T, Toh e A, Yokosawa H. Identification of ubiquitin-like protein-binding subunits of the 26S proteasome. Biochem Biophys Res Commun. 2002;296:813-9 pubmed
    ..By cross-linking experiments, Rpn1 and Rpn2 were identified as Ubl-binding subunits. Taken together, the results suggest that the Rpn1 and Rpn2 in the base subcomplex form the receptor for the ubiquitin-like protein. ..
  18. Satoh T, Saeki Y, Hiromoto T, Wang Y, Uekusa Y, Yagi H, et al. Structural basis for proteasome formation controlled by an assembly chaperone nas2. Structure. 2014;22:731-43 pubmed publisher
    ..We revealed that Nas2 binds to the Rpt5 subunit in a bivalent mode: the N-terminal helical domain of Nas2 masks the Rpt1-interacting surface of Rpt5, ..
  19. Verma R, Oania R, Fang R, Smith G, Deshaies R. Cdc48/p97 mediates UV-dependent turnover of RNA Pol II. Mol Cell. 2011;41:82-92 pubmed publisher
    ..These data reveal an intimate coupling of function between proteasomes and Cdc48 that we suggest is necessary to sustain processive degradation of unstable subunits of some macromolecular protein complexes. ..
  20. Saeki Y, Toh e A, Kudo T, Kawamura H, Tanaka K. Multiple proteasome-interacting proteins assist the assembly of the yeast 19S regulatory particle. Cell. 2009;137:900-13 pubmed publisher
    ..Our results indicate that the RP assembly is a highly organized and elaborate process orchestrated by multiple proteasome-dedicated chaperones. ..
  21. Kimura Y, Saeki Y, Yokosawa H, Polevoda B, Sherman F, Hirano H. N-Terminal modifications of the 19S regulatory particle subunits of the yeast proteasome. Arch Biochem Biophys. 2003;409:341-8 pubmed
    ..By using nat1, nat3, and mak3 deletion mutants, we found that 8 subunits, Rpt4, Rpt5, Rpt6, Rpn2, Rpn3, Rpn5, Rpn6, and Rpn8, were NatA substrates, and that 2 subunits, Rpt3 and Rpn11, were NatB ..
  22. Kalies K, Allan S, Sergeyenko T, Kroger H, Römisch K. The protein translocation channel binds proteasomes to the endoplasmic reticulum membrane. EMBO J. 2005;24:2284-93 pubmed
    ..Collectively, our data suggest that the Sec61 channel is a principal proteasome receptor in the ER membrane. ..
  23. Takeuchi J, Tamura T. Recombinant ATPases of the yeast 26S proteasome activate protein degradation by the 20S proteasome. FEBS Lett. 2004;565:39-42 pubmed
    ..Our finding, production of a functional subunit of the 19S regulatory particle in bacteria, is a simpler and technically advanced system to functionally characterize individual subunits. ..
  24. Kim I, Li Y, Muniz P, Rao H. Usa1 protein facilitates substrate ubiquitylation through two separate domains. PLoS ONE. 2009;4:e7604 pubmed publisher
    ..Usa1 may have another novel role in substrate ubiquitylation that is separate from the Hrd1 association. We conclude that Usa1 has two important roles in ERAD substrate ubiquitylation. ..
  25. Malik S, Shukla A, Sen P, Bhaumik S. The 19 s proteasome subcomplex establishes a specific protein interaction network at the promoter for stimulated transcriptional initiation in vivo. J Biol Chem. 2009;284:35714-24 pubmed publisher
    ..Together, these results provide significant insights as to how the 19 S proteasome subcomplex regulates the formation of the active transcription complex assembly (and, hence, transcriptional initiation) at the promoter in vivo. ..
  26. Yu Z, Livnat Levanon N, Kleifeld O, Mansour W, Nakasone M, Castaneda C, et al. Base-CP proteasome can serve as a platform for stepwise lid formation. Biosci Rep. 2015;35: pubmed publisher
  27. Annan R, Lee A, Reid I, Sayad A, Whiteway M, Hallett M, et al. A biochemical genomics screen for substrates of Ste20p kinase enables the in silico prediction of novel substrates. PLoS ONE. 2009;4:e8279 pubmed publisher
  28. De La Mota Peynado A, Lee S, Pierce B, Wani P, Singh C, Roelofs J. The proteasome-associated protein Ecm29 inhibits proteasomal ATPase activity and in vivo protein degradation by the proteasome. J Biol Chem. 2013;288:29467-81 pubmed publisher
    ..through chemical cross-linking that Ecm29 binds to, or in close proximity to, the proteasomal ATPase subunit Rpt5. Additionally, we show that Ecm29 preferentially associates with both mutant and nucleotide depleted proteasomes...
  29. Ferdous A, Gonzalez F, Sun L, Kodadek T, Johnston S. The 19S regulatory particle of the proteasome is required for efficient transcription elongation by RNA polymerase II. Mol Cell. 2001;7:981-91 pubmed
    ..Inhibition of the 20S proteolytic core of the proteasome has no effect on elongation. This work defines a nonproteolytic role for the 19S complex in RNAP II transcription. ..
  30. Schnall R, Mannhaupt G, Stucka R, Tauer R, Ehnle S, Schwarzlose C, et al. Identification of a set of yeast genes coding for a novel family of putative ATPases with high similarity to constituents of the 26S protease complex. Yeast. 1994;10:1141-55 pubmed
    ..b>YTA1, YTA2, YTA3 and YTA5 exhibit significant similarity to proteins involved in human immunodeficiency virus Tat-..