Gene Symbol: SCL1
Description: proteasome core particle subunit alpha 1
Alias: PRC2, proteasome core particle subunit alpha 1
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. Groll M, Ditzel L, Lowe J, Stock D, Bochtler M, Bartunik H, et al. Structure of 20S proteasome from yeast at 2.4 A resolution. Nature. 1997;386:463-71 pubmed
  2. Verma R, McDonald H, Yates J, Deshaies R. Selective degradation of ubiquitinated Sic1 by purified 26S proteasome yields active S phase cyclin-Cdk. Mol Cell. 2001;8:439-48 pubmed
    ..Activation of S-Cdk reported herein represents a complete reconstitution of the regulatory switch underlying the G1/S transition in budding yeast. ..
  3. 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. ..
  4. 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. ..
  5. 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
    ..Temperature sensitivity of one of these mutants, crl3-2, had been found to be suppressed by a mutation, SCL1-1, which resided in an alpha-type subunit of the 20S proteasome...
  6. McCusker J, Haber J. Cycloheximide-resistant temperature-sensitive lethal mutations of Saccharomyces cerevisiae. Genetics. 1988;119:303-15 pubmed
    ..We also describe two new methods for the enrichment of auxotrophic mutations from a wild-type yeast strain. ..
  7. Yashiroda H, Mizushima T, Okamoto K, Kameyama T, Hayashi H, Kishimoto T, et al. Crystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomes. Nat Struct Mol Biol. 2008;15:228-36 pubmed publisher
    ..The structure of the Dmp1-Dmp2-alpha5 complex reveals how this chaperone functions in proteasome assembly and why it dissociates from proteasome precursors before the beta-rings are assembled. ..
  8. Kusmierczyk A, Kunjappu M, Funakoshi M, Hochstrasser M. A multimeric assembly factor controls the formation of alternative 20S proteasomes. Nat Struct Mol Biol. 2008;15:237-44 pubmed publisher
    ..Our data demonstrate that Pba3-Pba4 orchestrates formation of a specific type of proteasome, the first example of a trans-acting factor that controls assembly of alternative proteasomal complexes. ..
  9. Denison C, Kodadek T. Toward a general chemical method for rapidly mapping multi-protein complexes. J Proteome Res. 2004;3:417-25 pubmed

More Information


  1. Demasi M, Silva G, Netto L. 20 S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-glutathionylated. J Biol Chem. 2003;278:679-85 pubmed
    ..The present results indicate that at the physiological level the yeast 20 S proteasome is regulated by its sulfhydryl content, thereby coupling intracellular redox signaling to proteasome-mediated proteolysis. ..
  2. 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
    ..A major location of proteasomal peptide cleavage activity was visualized in the NE-ER network, indicating that proteasomal degradation takes place mainly in this subcellular compartment in yeast. ..
  3. Silva G, Netto L, Discola K, Piassa Filho G, Pimenta D, Bárcena J, et al. Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome. FEBS J. 2008;275:2942-55 pubmed publisher
    ..These results indicate for the first time that 20S proteasome cysteinyl redox modification is a regulated mechanism coupled to enzymatic deglutathionylase activity. ..
  4. Prakash S, Inobe T, Hatch A, Matouschek A. Substrate selection by the proteasome during degradation of protein complexes. Nat Chem Biol. 2009;5:29-36 pubmed publisher
    ..In addition, our data provide a plausible explanation for how adaptor proteins can bind to otherwise stable proteins and target them for degradation. ..
  5. 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
    ..The wild-type scl1+ gene was isolated by screening subclones of the 35-kb region between TRP5 and LEU1 for restoration of the ts ..
  6. 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. ..
  7. 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. ..
  8. Narayanan A, Pullepu D, Reddy P, Uddin W, Kabir M. Defects in Protein Folding Machinery Affect Cell Wall Integrity and Reduce Ethanol Tolerance in S. cerevisiae. Curr Microbiol. 2016;73:38-45 pubmed publisher
    ..Genetic and proteomic analyses showed that the yeast genes RPS6A (ribosomal protein), SCL1 (proteasomal subunit) and TDH3 (glyceraldehyde-3-phosphate dehydrogenase) on overexpression, improved the growth of ..
  9. 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. ..
  10. 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. ..
  11. Kalderon B, Kogan G, Bubis E, Pines O. Cytosolic Hsp60 can modulate proteasome activity in yeast. J Biol Chem. 2015;290:3542-51 pubmed publisher
    ..Even mutant Hsp60 proteins, lacking chaperone activity, were still capable of proteasome inhibition. The results support the hypothesis that localization of Hsp60 to the cytosol may modulate proteasome activity according to cell need. ..
  12. Wani P, Rowland M, Ondracek A, Deeds E, Roelofs J. Maturation of the proteasome core particle induces an affinity switch that controls regulatory particle association. Nat Commun. 2015;6:6384 pubmed publisher
    ..Our work thus provides mechanistic insights into a crucial step in proteasome biogenesis. ..
  13. Rosenzweig R, Osmulski P, Gaczynska M, Glickman M. The central unit within the 19S regulatory particle of the proteasome. Nat Struct Mol Biol. 2008;15:573-80 pubmed publisher
    ..Similar pairing of units is found in unfoldases and nuclear transporters, exposing common features of these protein nanomachines. ..
  14. Baugh J, Viktorova E, Pilipenko E. Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination. J Mol Biol. 2009;386:814-27 pubmed publisher
    ..Collectively, these findings suggest a significant contribution of the ubiquitin-independent proteasome degradation pathway to the regulation of protein homeostasis in eukaryotes. ..