Genomes and Genes
Gene Symbol: RPT1
Description: proteasome regulatory particle base subunit RPT1
Alias: CIM5, YTA3, proteasome regulatory particle base subunit RPT1
Species: Saccharomyces cerevisiae S288c
- 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. ..
- Glickman M, Rubin D, Fried V, Finley D. The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol Cell Biol. 1998;18:3149-62 pubmed..Six of the subunits have sequence features of ATPases (Rpt1 to Rpt6)...
- 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. ..
- 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..A hetero-hexameric ATPase ring, containing subunits Rpt1-6, is situated within the base subassembly of the regulatory particle...
- 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. ..
- 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..Hsm3 associates with 19S subcomplexes via a carboxy-terminal domain of the Rpt1 base subunit but is missing in the final 26S proteasome...
- Takagi K, Kim S, Yukii H, Ueno M, Morishita R, Endo Y, et al. Structural basis for specific recognition of Rpt1p, an ATPase subunit of 26 S proteasome, by proteasome-dedicated chaperone Hsm3p. J Biol Chem. 2012;287:12172-82 pubmed publisher..Hsm3, a 19 S RP dedicated chaperone, transiently binds to the C-terminal domain of the Rpt1 subunit and forms a tetrameric complex, Hsm3-Rpt1-Rpt2-Rpn1, during maturation of the ATPase ring of 19 S RP...
- Romero Perez L, Chen L, Lambertson D, Madura K. Sts1 can overcome the loss of Rad23 and Rpn10 and represents a novel regulator of the ubiquitin/proteasome pathway. J Biol Chem. 2007;282:35574-82 pubmed..Despite these proteolytic defects, overall proteasome activity was increased in sts1-2. We propose that Sts1 is a new regulatory factor in the ubiquitin/proteasome pathway that controls the turnover of proteasome substrates...
- 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..YTA1, YTA2, YTA3 and YTA5 exhibit significant similarity to proteins involved in human immunodeficiency virus Tat-mediated gene ..
- Geng F, Tansey W. Similar temporal and spatial recruitment of native 19S and 20S proteasome subunits to transcriptionally active chromatin. Proc Natl Acad Sci U S A. 2012;109:6060-5 pubmed publisher..We find that proteasome subunits Rpt1, Rpt4, Rpn8, Rpn12, Pre6, and Pre10 are recruited to GAL10 rapidly upon galactose induction...
- NEAL S, Mak R, Bennett E, HAMPTON R. A Cdc48 "Retrochaperone" Function Is Required for the Solubility of Retrotranslocated, Integral Membrane Endoplasmic Reticulum-associated Degradation (ERAD-M) Substrates. J Biol Chem. 2017;292:3112-3128 pubmed publisher..Thus, in addition to the long known ATP-dependent extraction of ERAD substrates during retrotranslocation, the Cdc48 complex is generally and critically needed for the solubility of retrotranslocated ERAD-M intermediates. ..
- van Nocker S, Sadis S, Rubin D, Glickman M, Fu H, Coux O, et al. The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover. Mol Cell Biol. 1996;16:6020-8 pubmed..Collectively, these data suggest that Mcb1 is not the sole factor involved in ubiquitin recognition by the 26S proteasome and that Mcb1 may interact with only a subset of ubiquitinated substrates. ..
- Takeuchi J, Fujimuro M, Yokosawa H, Tanaka K, Toh e A. Rpn9 is required for efficient assembly of the yeast 26S proteasome. Mol Cell Biol. 1999;19:6575-84 pubmed..These results indicate that Rpn9 is needed for incorporating Rpn10 into the 26S proteasome and that Rpn9 participates in the assembly and/or stability of the 26S proteasome. ..
- Kaiser M, RÃ¶misch K. Proteasome 19S RP binding to the Sec61 channel plays a key role in ERAD. PLoS ONE. 2015;10:e0117260 pubmed publisher..Our data suggest that the interaction between the 19S RP and the Sec61 channel is essential for the export of specific substrates from the ER to the cytosol for proteasomal degradation. ..
- Ha S, Ju D, Xie Y. The N-terminal domain of Rpn4 serves as a portable ubiquitin-independent degron and is recognized by specific 19S RP subunits. Biochem Biophys Res Commun. 2012;419:226-31 pubmed publisher..Using a photo-crosslinking-label transfer method, we captured three 19S RP subunits (Rpt1, Rpn2 and Rpn5) that bind the Ub-independent degron of Rpn4...
- Tongaonkar P, Chen L, Lambertson D, Ko B, Madura K. Evidence for an interaction between ubiquitin-conjugating enzymes and the 26S proteasome. Mol Cell Biol. 2000;20:4691-8 pubmed..Purified proteasomes can ligate ubiquitin to a test substrate without the addition of exogenous E2 protein, suggesting that the ubiquitylation of some proteolytic substrates might be directly coupled to degradation by the proteasome. ..
- Xie Y, Varshavsky A. Physical association of ubiquitin ligases and the 26S proteasome. Proc Natl Acad Sci U S A. 2000;97:2497-502 pubmed..These and related results suggest that a substrate-bound Ub ligase participates in the delivery of substrates to the proteasome, because of affinity between the ligase's E3 component and specific proteins of the 19S particle. ..
- Rubin D, van Nocker S, Glickman M, Coux O, Wefes I, Sadis S, et al. ATPase and ubiquitin-binding proteins of the yeast proteasome. Mol Biol Rep. 1997;24:17-26 pubmed..Our data suggest that the recognition of ubiquitin conjugates by the proteasome is a complex process which must involve proteins other than Mcb1. ..
- 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. ..
- Tone Y, Tanahashi N, Tanaka K, Fujimuro M, Yokosawa H, Toh e A. Nob1p, a new essential protein, associates with the 26S proteasome of growing saccharomyces cerevisiae cells. Gene. 2000;243:37-45 pubmed..found only in proteasomal fractions in a glycerol gradient centrifugation profile and immuno-coprecipitated with Rpt1, which is an ATPase component of the yeast proteasomes...
- Wang L, Mao X, Ju D, Xie Y. Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase. J Biol Chem. 2004;279:55218-23 pubmed..Furthermore, we showed that deletion of UBR2 exhibited a strong synthetic growth defect with a mutation in the Rpt1 proteasome subunit when Rpn4 was overexpressed...
- Yu V, Baskerville C, Grünenfelder B, Reed S. A kinase-independent function of Cks1 and Cdk1 in regulation of transcription. Mol Cell. 2005;17:145-51 pubmed..However, it is independent of the protein kinase activity of Cdc28. In the absence of Cks1, neither Cdc28 nor the proteasome can be recruited. Consequently, there is a failure to maintain efficient transcription. ..
- Papa F, Amerik A, Hochstrasser M. Interaction of the Doa4 deubiquitinating enzyme with the yeast 26S proteasome. Mol Biol Cell. 1999;10:741-56 pubmed..Together, these data support a model in which Doa4 promotes proteolysis through removal of ubiquitin from proteolytic intermediates on the proteasome before or after initiation of substrate breakdown. ..
- Ishii T, Funakoshi M, Kobayashi H. Yeast Pth2 is a UBL domain-binding protein that participates in the ubiquitin-proteasome pathway. EMBO J. 2006;25:5492-503 pubmed..These results suggest that Pth2 negatively regulates the UBL-UBA protein-mediated shuttling pathway in the ubiquitin-proteasome system. ..
- Takeuchi J, Toh e A. Genetic evidence for interaction between components of the yeast 26S proteasome: combination of a mutation in RPN12 (a lid component gene) with mutations in RPT1 (an ATPase gene) causes synthetic lethality. Mol Gen Genet. 1999;262:145-53 pubmed..Among the candidates recovered was a new allele of RPT1 (formerly CIM5)...
- Chen L, Madura K. Centrin/Cdc31 is a novel regulator of protein degradation. Mol Cell Biol. 2008;28:1829-40 pubmed..These findings reveal for the first time a new role for centrin/Cdc31 in protein degradation. ..
- Marques A, Glanemann C, Ramos P, Dohmen R. The C-terminal extension of the beta7 subunit and activator complexes stabilize nascent 20 S proteasomes and promote their maturation. J Biol Chem. 2007;282:34869-76 pubmed..Together these data demonstrate that Blm10 and the 19 S activator have a partially redundant function in stabilizing nascent 20 S proteasomes and in promoting their activation. ..
- 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 pubmedA family of ATPases resides within the regulatory particle of the proteasome. These proteins (Rpt1-Rpt6) have been proposed to mediate substrate unfolding, which may be required for translocation of substrates through the channel that ..
- Hatanaka A, Chen B, Sun J, Mano Y, Funakoshi M, Kobayashi H, et al. Fub1p, a novel protein isolated by boundary screening, binds the proteasome complex. Genes Genet Syst. 2011;86:305-14 pubmed..Finally, boundary assay showed that human PSMF1 also exhibited boundary establishment activity in yeast. Our results defined the functional correlation between Fub1p and PSMF1. ..
- Chien C, Chen R. Cdc48 chaperone and adaptor Ubx4 distribute the proteasome in the nucleus for anaphase proteolysis. J Biol Chem. 2013;288:37180-91 pubmed publisher..Our data propose that Cdc48-Ubx4 acts on the proteasome and uses the chaperone activity to promote its nuclear distribution, thereby optimizing the proteasome level for efficient degradation of mitotic regulators...
- Sun L, Johnston S, Kodadek T. Physical association of the APIS complex and general transcription factors. Biochem Biophys Res Commun. 2002;296:991-9 pubmed..These data add to the growing body of evidence that the APIS complex has a role in transcription, independent of its role in proteolysis and, furthermore, argues that it functions in association with the general transcription complex. ..
- 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. ..
- 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. ..
- Archer C, Burdine L, Liu B, Ferdous A, Johnston S, Kodadek T. Physical and functional interactions of monoubiquitylated transactivators with the proteasome. J Biol Chem. 2008;283:21789-98 pubmed publisher..cross-linking techniques, we show that ubiquitin contacts the ATPase complex directly, apparently via Rpn1 and Rpt1. This interaction results in the dissociation of the activation domain-ATPase complex via an allosteric process...
- Funakoshi M, Li X, Velichutina I, Hochstrasser M, Kobayashi H. Sem1, the yeast ortholog of a human BRCA2-binding protein, is a component of the proteasome regulatory particle that enhances proteasome stability. J Cell Sci. 2004;117:6447-54 pubmed..Our data suggest a potential mechanism for this protein-protein stabilization and also suggest that an intact proteasomal regulatory particle is required for responses to DNA damage. ..
- Chuang S, Chen L, Lambertson D, Anand M, Kinzy T, Madura K. Proteasome-mediated degradation of cotranslationally damaged proteins involves translation elongation factor 1A. Mol Cell Biol. 2005;25:403-13 pubmed..eEF1A interacted with the proteasome subunit Rpt1, and the turnover of nascent damaged proteins was deficient in rpt1...
- 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. ..
- Funakoshi M, Sasaki T, Nishimoto T, Kobayashi H. Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome. Proc Natl Acad Sci U S A. 2002;99:745-50 pubmed..We discuss a possible role of adaptor function of Dsk2p via its UbL and UBA domains in the ubiquitin-proteasome pathway. ..
- Mullen J, Chen C, Brill S. Wss1 is a SUMO-dependent isopeptidase that interacts genetically with the Slx5-Slx8 SUMO-targeted ubiquitin ligase. Mol Cell Biol. 2010;30:3737-48 pubmed publisher..The results suggest that Wss1 is a SUMO-dependent isopeptidase that acts on sumoylated substrates as they undergo proteasomal degradation. ..
- Jager S, Strayle J, Heinemeyer W, Wolf D. Cic1, an adaptor protein specifically linking the 26S proteasome to its substrate, the SCF component Cdc4. EMBO J. 2001;20:4423-31 pubmed..Cic1 interacts in vitro and in vivo with Cdc4, suggesting a function as a new kind of substrate recruiting factor or adaptor associated with the proteasome. ..
- Lambertson D, Chen L, Madura K. Investigating the importance of proteasome-interaction for Rad23 function. Curr Genet. 2003;42:199-208 pubmed..These results suggest that the localization of Rad23 to the proteasome, either by its UbL domain, or following ubiquitination of an amino-terminal ubiquitin moiety (Ub-rad23), is necessary for full activity. ..
- Suzuki T, Park H, Kwofie M, Lennarz W. Rad23 provides a link between the Png1 deglycosylating enzyme and the 26 S proteasome in yeast. J Biol Chem. 2001;276:21601-7 pubmed..We propose a model in which Rad23p functions as an escort protein to link the 26 S proteasome with proteins such as Rad4p or Png1p to regulate their cellular activities. ..
- Kimura Y, Yashiroda H, Kudo T, Koitabashi S, Murata S, Kakizuka A, et al. An inhibitor of a deubiquitinating enzyme regulates ubiquitin homeostasis. Cell. 2009;137:549-59 pubmed publisher..We propose that free ubiquitin chains function as a ubiquitin reservoir that allows maintenance of monomeric ubiquitins at adequate levels under normal conditions and rapid supply for substrate conjugation under stress conditions. ..
- Pan Y, Sun M, Wohlschlegel J, Reed S. Cks1 enhances transcription efficiency at the GAL1 locus by linking the Paf1 complex to the 19S proteasome. Eukaryot Cell. 2013;12:1192-201 pubmed publisher..We further found that Cks1 in this capacity serves as an adaptor allowing Rtf1 to recruit 19S proteasome particles, shown to be required for efficient RNA production from some rapidly inducible genes such as GAL1...
- Park S, Li X, Kim H, Singh C, Tian G, Hoyt M, et al. Reconfiguration of the proteasome during chaperone-mediated assembly. Nature. 2013;497:512-6 pubmed publisherThe proteasomal ATPase ring, comprising Rpt1-Rpt6, associates with the heptameric ?-ring of the proteasome core particle (CP) in the mature proteasome, with the Rpt carboxy-terminal tails inserting into pockets of the ?-ring...
- Chen L, Madura K. Evidence for distinct functions for human DNA repair factors hHR23A and hHR23B. FEBS Lett. 2006;580:3401-8 pubmed..We also determined that hHR23A and hHR23B could be co-purified with unique proteolytic and stress-responsive factors from human breast cancer tissues, indicating that they have unique functions in vivo. ..
- Ehlinger A, Park S, Fahmy A, Lary J, Cole J, Finley D, et al. Conformational dynamics of the Rpt6 ATPase in proteasome assembly and Rpn14 binding. Structure. 2013;21:753-65 pubmed publisher..RP triphosphatase proteins (Rpt1-Rpt6), which are critical for substrate translocation into the CP, bind chaperone-like proteins (Hsm3, Nas2, Nas6, ..
- Demarini D, Papa F, Swaminathan S, Ursic D, Rasmussen T, Culbertson M, et al. The yeast SEN3 gene encodes a regulatory subunit of the 26S proteasome complex required for ubiquitin-dependent protein degradation in vivo. Mol Cell Biol. 1995;15:6311-21 pubmed
- Marshall R, McLoughlin F, Vierstra R. Autophagic Turnover of Inactive 26S Proteasomes in Yeast Is Directed by the Ubiquitin Receptor Cue5 and the Hsp42 Chaperone. Cell Rep. 2016;16:1717-1732 pubmed publisher..Together, Cue5 and Hsp42 provide a quality control checkpoint in yeast directed at recycling dysfunctional 26S proteasomes. ..
- 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. ..
- Liang R, Chen L, Ko B, Shen Y, Li Y, Chen B, et al. Rad23 interaction with the proteasome is regulated by phosphorylation of its ubiquitin-like (UbL) domain. J Mol Biol. 2014;426:4049-60 pubmed publisher..Strikingly, threonine 75 in human HR23B also regulates interaction with the proteasome, suggesting that phosphorylation is a conserved mechanism for controlling Rad23/proteasome interaction. ..
- 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. ..
- Chuang S, Madura K. Saccharomyces cerevisiae Ub-conjugating enzyme Ubc4 binds the proteasome in the presence of translationally damaged proteins. Genetics. 2005;171:1477-84 pubmed..We showed that the translation elongation factor eEF1A and the proteasome subunit Rpt1 play a central role in the translocation of nascent-damaged proteins to the proteasome...
- Schauber C, Chen L, Tongaonkar P, Vega I, Lambertson D, Potts W, et al. Rad23 links DNA repair to the ubiquitin/proteasome pathway. Nature. 1998;391:715-8 pubmed..proteins glutathione S-transferase (GST)-Rad23 and Rad4-haemagglutinin (HA), and the proteasome subunits Cim3 and Cim5, cofractionate through consecutive chromatography steps...
- Joshi K, Chen L, Torres N, Tournier V, Madura K. A proteasome assembly defect in rpn3 mutants is associated with Rpn11 instability and increased sensitivity to stress. J Mol Biol. 2011;410:383-99 pubmed publisher..These studies suggest that Rpn11 is stabilized following its incorporation into proteasomes. The instability of Rpn11 and the defects of rpn3 mutants are apparently caused by a failure to recruit Rpn11 into mature proteasomes. ..
- Ghislain M, Udvardy A, Mann C. S. cerevisiae 26S protease mutants arrest cell division in G2/metaphase. Nature. 1993;366:358-62 pubmedWe isolated two mutants from the yeast Saccharomyces cerevisiae, cim3-1 and cim5-1, that arrest cell division in G2/metaphase at 37 degrees C. CIM3 (identical to SUG1; ref...
- Panasenko O, David F, Collart M. Ribosome association and stability of the nascent polypeptide-associated complex is dependent upon its own ubiquitination. Genetics. 2009;181:447-60 pubmed publisher..Finally, our study demonstrated an interaction of EGD/NAC with the proteasome and revealed the importance of the Not4p E3 ligase, responsible for EGD/NAC ubiquitination, in this association. ..
- Fujimuro M, Tanaka K, Yokosawa H, Toh e A. Son1p is a component of the 26S proteasome of the yeast Saccharomyces cerevisiae. FEBS Lett. 1998;423:149-54 pubmed..The resultant precipitate contained Nin1p, Sun1p, TBP1, and the 20S proteasome. Combining genetic and biochemical results together, we concluded that Son1p is a component of the yeast 26S proteasome. ..
- 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. ..
- Kaiser P, Moncollin V, Clarke D, Watson M, Bertolaet B, Reed S, et al. Cyclin-dependent kinase and Cks/Suc1 interact with the proteasome in yeast to control proteolysis of M-phase targets. Genes Dev. 1999;13:1190-202 pubmed..Stabilization of Pds1 is partially responsible for the metaphase arrest phenotype of cks1 mutants because deletion of PDS1 partially relieves the metaphase block in these mutants. ..
- Hosomi A, Tanabe K, Hirayama H, Kim I, Rao H, Suzuki T. Identification of an Htm1 (EDEM)-dependent, Mns1-independent Endoplasmic Reticulum-associated Degradation (ERAD) pathway in Saccharomyces cerevisiae: application of a novel assay for glycoprotein ERAD. J Biol Chem. 2010;285:24324-34 pubmed publisher..The newly established RTL assay will allow us to gain further insight into the mechanisms involved in the Png1-dependent ERAD-L pathway. ..
- Enenkel C, Lehmann A, Kloetzel P. Subcellular distribution of proteasomes implicates a major location of protein degradation in the nuclear envelope-ER network in yeast. EMBO J. 1998;17:6144-54 pubmed..complex of the 26S proteasome, Pre6/YOL038w, as well as an ATPase-type subunit of the regulatory 19S cap complex, Cim5/YOL145w, were tagged with GFP. Both chimeras were shown to be incorporated completely into active 26S proteasomes...