Gene Symbol: RPT6
Description: proteasome regulatory particle base subunit RPT6
Alias: CIM3, CRL3, SCB68, SUG1, proteasome regulatory particle base subunit RPT6
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. 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. ..
  2. Sulahian R, Sikder D, Johnston S, Kodadek T. The proteasomal ATPase complex is required for stress-induced transcription in yeast. Nucleic Acids Res. 2006;34:1351-7 pubmed
    b>Sug1 and Sug2 are two of six ATPases in the 19S regulatory particle of the 26S proteasome. We have shown previously that these proteins play a non-proteolytic role in the transcription of the GAL genes in yeast...
  3. 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. ..
  4. 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
    ..we use 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...
  5. 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. ..
  6. Russell S, Steger K, Johnston S. Subcellular localization, stoichiometry, and protein levels of 26 S proteasome subunits in yeast. J Biol Chem. 1999;274:21943-52 pubmed
    ..subcellular localization of two ATPase components of the regulatory complex of the proteasome, Sug2/Rpt4 and Sug1/Rpt6, and a subunit of the 20 S proteasome, Pre1, were determined by immunofluorescence...
  7. 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)...
  8. McCusker J, Haber J. Cycloheximide-resistant temperature-sensitive lethal mutations of Saccharomyces cerevisiae. Genetics. 1988;119:303-15 pubmed
    ..groups exhibit similar temperature-sensitive phenotypes, an extragenic suppressor of the ts lethality of crl3 does not relieve the ts lethality of most other crl mutants...
  9. 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. ..

More Information


  1. Fehlker M, Wendler P, Lehmann A, Enenkel C. Blm3 is part of nascent proteasomes and is involved in a late stage of nuclear proteasome assembly. EMBO Rep. 2003;4:959-63 pubmed
    ..On the basis of biochemical fractionation experiments combined with in vivo localization studies, we propose that Blm3 joins nascent CPs inside the nucleus to coordinate late stages of proteasome assembly in yeast. ..
  2. Gerlinger U, Gückel R, Hoffmann M, Wolf D, Hilt W. Yeast cycloheximide-resistant crl mutants are proteasome mutants defective in protein degradation. Mol Biol Cell. 1997;8:2487-99 pubmed
    ..We cloned the CRL3 gene by complementation and found CRL3 to be identical to the SUG1/CIM3 gene coding for a subunit of the 19S cap complex of the 26S proteasome...
  3. Xu Q, Singer R, Johnston G. Sug1 modulates yeast transcription activation by Cdc68. Mol Cell Biol. 1995;15:6025-35 pubmed
    ..We report here the molecular characterization of mutations in one suppressor gene, the previously identified SUG1 gene. The Sug1 protein has been implicated in both transcriptional regulation and proteolysis...
  4. Kim Y, Bjorklund S, Li Y, Sayre M, Kornberg R. A multiprotein mediator of transcriptional activation and its interaction with the C-terminal repeat domain of RNA polymerase II. Cell. 1994;77:599-608 pubmed
    ..including the three subunits of TFIIF and other polypeptides cross-reactive with antisera against GAL11, SUG1, SRB2, SRB4, SRB5, and SRB6 proteins...
  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
    ..Our results demonstrate that proteasomal RP biogenesis requires multiple, functionally overlapping chaperones and suggest a model in which subunits form specific subcomplexes that then assemble into the base. ..
  6. 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. ..
  7. Jeong C, Yang S, Xie Y, Zhang L, Johnston S, Kodadek T. Evidence that Gal11 protein is a target of the Gal4 activation domain in the mediator. Biochemistry. 2001;40:9421-7 pubmed
  8. 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. ..
  9. 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
    ..The Rpt proteins with the strongest assembly phenotypes, Rpt4 and Rpt6, were absent from BP1...
  10. 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. ..
  11. 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
    ..First, yeast strains carrying alleles of SUG1 and SUG2, encoding 19S components, exhibit phenotypes indicative of elongation defects...
  12. Archer C, Delahodde A, Gonzalez F, Johnston S, Kodadek T. Activation domain-dependent monoubiquitylation of Gal4 protein is essential for promoter binding in vivo. J Biol Chem. 2008;283:12614-23 pubmed publisher
    ..This is because of the activity of the proteasomal ATPases, including Sug1/Rpt6, which bind to Gal4D via the remainder of the AD and strip it off of DNA...
  13. Fujii K, Kitabatake M, Sakata T, Ohno M. 40S subunit dissociation and proteasome-dependent RNA degradation in nonfunctional 25S rRNA decay. EMBO J. 2012;31:2579-89 pubmed publisher
  14. Kingsbury J, McCusker J. Homoserine toxicity in Saccharomyces cerevisiae and Candida albicans homoserine kinase (thr1Delta) mutants. Eukaryot Cell. 2010;9:717-28 pubmed publisher
    ..Since the doa4Delta and proteasome mutants identified have reduced ubiquitin- and/or proteasome-mediated proteolysis, the degradation of a particular protein or subset of proteins likely contributes to homoserine toxicity...
  15. 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. ..
  16. Swaffield J, Melcher K, Johnston S. A highly conserved ATPase protein as a mediator between acidic activation domains and the TATA-binding protein. Nature. 1995;374:88-91 pubmed
    ..We have previously shown genetically that Sug1 interacts with the AD of the yeast activator Ga14...
  17. 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. ..
  18. 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
    ..The remaining two subunits, Rpt2 and Rpt6, with empty or only partially occupied nucleotide pocket exhibit pronounced conformational changes in the AAA-..
  19. Chouduri A, Tokumoto T, Dohra H, Ushimaru T, Yamada S. Functional and biochemical characterization of the 20S proteasome in a yeast temperature-sensitive mutant, rpt6-1. BMC Biochem. 2008;9:20 pubmed publisher
    b>Rpt6-1 is a thermosensitive yeast mutant with a deletion of a gene encoding a regulatory subunit of the 26S proteasome, RPT6, which is able to grow at 25 degrees C but not at 37 degrees C...
  20. 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. ..
  21. 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. ..
  22. 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 publisher
    The 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...
  23. Faza M, Kemmler S, Jimeno S, González Aguilera C, Aguilera A, Hurt E, et al. Sem1 is a functional component of the nuclear pore complex-associated messenger RNA export machinery. J Cell Biol. 2009;184:833-46 pubmed publisher
    ..Thus, Sem1 is a versatile protein that might stabilize multiple protein complexes involved in diverse pathways. ..
  24. 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. ..
  25. Russell S, Gonzalez F, Joshua Tor L, Johnston S. Selective chemical inactivation of AAA proteins reveals distinct functions of proteasomal ATPases. Chem Biol. 2001;8:941-50 pubmed
    ..Mutation of a threonine in the active site of Sug1/Rpt6 or Sug2/Rpt4 to a cysteine sensitizes these proteins to inactivation through alkylation by the sulfhydryl modifying ..
  26. Sokolova V, Li F, Polovin G, Park S. Proteasome Activation is Mediated via a Functional Switch of the Rpt6 C-terminal Tail Following Chaperone-dependent Assembly. Sci Rep. 2015;5:14909 pubmed publisher
    ..Six ATPases (Rpt1-Rpt6) of the RP form a hexameric Rpt ring and interact with the heptameric α ring (α1-α7) of the CP via the Rpt ..
  27. Cohen M, Stutz F, Belgareh N, Haguenauer Tsapis R, Dargemont C. Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23. Nat Cell Biol. 2003;5:661-7 pubmed
    ..This probably contributes to maintaining and adapting a Sec23 expression level that is compatible with an efficient secretion pathway, and consequently with cell growth and viability. ..
  28. 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, and ..
  29. 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. ..
  30. Melcher K, Johnston S. GAL4 interacts with TATA-binding protein and coactivators. Mol Cell Biol. 1995;15:2839-48 pubmed
    ..from a crude extract: the negative regulator GAL80, the TATA-binding protein (TBP), and the putative coactivators SUG1 and ADA2. TFIIB was not retained...
  31. Russell S, Johnston S. Evidence that proteolysis of Gal4 cannot explain the transcriptional effects of proteasome ATPase mutations. J Biol Chem. 2001;276:9825-31 pubmed
    ..A search for extragenic suppressors of gal4D identified recessive mutations in the SUG1 and SUG2 genes, which encode ATPases of the 19S regulatory complex of the proteasome...
  32. 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. ..
  33. 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. ..
  34. 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. ..
  35. 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. ..
  36. 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. ..
  37. Laporte D, Salin B, Daignan Fornier B, Sagot I. Reversible cytoplasmic localization of the proteasome in quiescent yeast cells. J Cell Biol. 2008;181:737-45 pubmed publisher
    ..Finally, we observe conserved formation and mobilization of these PSGs in the evolutionary distant yeast Schizosaccharomyces pombe. This conservation implies a broad significance for these proteasome reserves. ..
  38. 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
    ..Thus, Nas2 operates as a proteasome activation blocker, offering a checkpoint during the formation of the 19S ATPase prior to its docking onto the proteolytic 20S core particle. ..
  39. 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
    ..The fusion proteins glutathione S-transferase (GST)-Rad23 and Rad4-haemagglutinin (HA), and the proteasome subunits Cim3 and Cim5, cofractionate through consecutive chromatography steps...
  40. Lee D, Ezhkova E, Li B, Pattenden S, Tansey W, Workman J. The proteasome regulatory particle alters the SAGA coactivator to enhance its interactions with transcriptional activators. Cell. 2005;123:423-36 pubmed
    ..These results indicate that the 19S RP modulates SAGA complex using its ATPase components, thereby facilitating subsequent transcription events at promoters. ..
  41. Ezhkova E, Tansey W. Proteasomal ATPases link ubiquitylation of histone H2B to methylation of histone H3. Mol Cell. 2004;13:435-42 pubmed
    ..Here, we demonstrate that proteasomal ATPases Rpt4 and Rpt6 function to connect these two histone modifications...
  42. 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. ..
  43. 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. ..
  44. Zhang N, Quan Z, Rash B, Oliver S. Synergistic effects of TOR and proteasome pathways on the yeast transcriptome and cell growth. Open Biol. 2013;3:120137 pubmed publisher
    ..These data suggest that the proteasome and the TOR signalling pathway synergistically regulate a significant portion of the genome to coordinate cell growth and starvation response. ..
  45. 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. ..
  46. Ferdous A, Sikder D, Gillette T, Nalley K, Kodadek T, Johnston S. The role of the proteasomal ATPases and activator monoubiquitylation in regulating Gal4 binding to promoters. Genes Dev. 2007;21:112-23 pubmed
    ..The fact that monoubiquitylated activator is resistant to the "stripping" activity of the proteasomal ATPases may explain, in part, why some activators require this modification in order to function efficiently. ..
  47. Xie Y, Varshavsky A. UFD4 lacking the proteasome-binding region catalyses ubiquitination but is impaired in proteolysis. Nat Cell Biol. 2002;4:1003-7 pubmed
    ..Here we advance this analysis for UFD4 and show that it interacts with RPT4 and RPT6, two subunits of the 19S particle...
  48. Zuin A, Bichmann A, Isasa M, Puig Sàrries P, Díaz L, Crosas B. Rpn10 monoubiquitination orchestrates the association of the ubiquilin-type DSK2 receptor with the proteasome. Biochem J. 2015;472:353-65 pubmed publisher
    ..Interestingly, Rpn10-ubiquitin, with an inactivated ubiquitin-interacting motif (UIM), and Dsk2(I45S), with an inactive ubiquitin-like domain (UBL), show temperature-dependent phenotypes with multiple functional interactions. ..
  49. Hrizo S, Gusarova V, Habiel D, Goeckeler J, Fisher E, Brodsky J. The Hsp110 molecular chaperone stabilizes apolipoprotein B from endoplasmic reticulum-associated degradation (ERAD). J Biol Chem. 2007;282:32665-75 pubmed
    ..This study indicates that chaperones within distinct complexes can play unique roles during ER-associated degradation (ERAD), establishes a role for Sse1/Hsp110 in ERAD, and identifies Hsp110 as a target to lower cholesterol. ..
  50. Chew B, Siew W, Xiao B, Lehming N. Transcriptional activation requires protection of the TATA-binding protein Tbp1 by the ubiquitin-specific protease Ubp3. Biochem J. 2010;431:391-9 pubmed publisher
    ..Chromatin immunoprecipitation showed that Ubp3 was recruited to the GAL1 and HIS3 promoters upon the induction of the respective gene, indicating that protection of promoter-bound Tbp1 by Ubp3 is required for transcriptional activation. ..
  51. Russell S, Reed S, Huang W, Friedberg E, Johnston S. The 19S regulatory complex of the proteasome functions independently of proteolysis in nucleotide excision repair. Mol Cell. 1999;3:687-95 pubmed
    ..Surprisingly, blockage of protein degradation by the proteasome has no effect on the efficiency of NER. This establishes that the regulatory complex of the proteasome has a function independent of protein degradation. ..
  52. Balzi E, Chen W, Capieaux E, McCusker J, Haber J, Goffeau A. The suppressor gene scl1+ of Saccharomyces cerevisiae is essential for growth. Gene. 1989;83:271-9 pubmed
    ..SCL-1 mutation is a dominant suppressor of the cycloheximide-resistant, temperature-sensitive (ts) lethal mutation, crl3 [McCusker and Haber, Genetics 119 (1988a) 303-315]...
  53. 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
  54. 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. ..
  55. Laribee R, Shibata Y, Mersman D, Collins S, Kemmeren P, Roguev A, et al. CCR4/NOT complex associates with the proteasome and regulates histone methylation. Proc Natl Acad Sci U S A. 2007;104:5836-41 pubmed
    ..These studies implicate CCR4/NOT in the regulation of H3K4me3 through a ubiquitin-dependent pathway that likely involves the proteasome. ..
  56. Gillette T, Huang W, Russell S, Reed S, Johnston S, Friedberg E. The 19S complex of the proteasome regulates nucleotide excision repair in yeast. Genes Dev. 2001;15:1528-39 pubmed
    ..The 19S regulatory complex of the yeast proteasome functions in nucleotide excision repair independent of proteolysis. ..
  57. Russell S, Sathyanarayana U, Johnston S. Isolation and characterization of SUG2. A novel ATPase family component of the yeast 26 S proteasome. J Biol Chem. 1996;271:32810-7 pubmed
    ..One of these genes, SUG1, encodes a member of a large family of putative ATPases, the Conserved ATPase containing Domain (CAD) proteins (..
  58. Makino Y, Yamano K, Kanemaki M, Morikawa K, Kishimoto T, Shimbara N, et al. SUG1, a component of the 26 S proteasome, is an ATPase stimulated by specific RNAs. J Biol Chem. 1997;272:23201-5 pubmed
    b>SUG1 is an integral component of the 26 S proteasome. Belonging to a novel putative ATPase family, it shares four conserved motifs characteristic of ATP-dependent DNA/RNA helicases...
  59. Marquez Lona E, Torres Machorro A, Gonzales F, Pillus L, Patrick G. Phosphorylation of the 19S regulatory particle ATPase subunit, Rpt6, modifies susceptibility to proteotoxic stress and protein aggregation. PLoS ONE. 2017;12:e0179893 pubmed publisher
    ..We previously reported that Rpt6, the ATPase subunit of the 19S regulatory particle (RP) of the 26S proteasome, is phosphorylated in mammalian ..