Genomes and Genes
Gene Symbol: SCL1
Description: proteasome core particle subunit alpha 1
Species: Saccharomyces cerevisiae S288c
- Structure of 20S proteasome from yeast at 2.4 A resolutionM Groll
Max Planck Institut fur Biochemie, Martinsreid, Germany
Nature 386:463-71. 1997....
- Selective degradation of ubiquitinated Sic1 by purified 26S proteasome yields active S phase cyclin-CdkR Verma
Howard Hughes Medical Institute, Division of Biology, California Institute of Technology, Pasadena, CA 91125, USA
Mol Cell 8:439-48. 2001..Activation of S-Cdk reported herein represents a complete reconstitution of the regulatory switch underlying the G1/S transition in budding yeast...
- The C-terminal extension of the beta7 subunit and activator complexes stabilize nascent 20 S proteasomes and promote their maturationAntónio J Marques
Institute for Genetics, University of Cologne, Zulpicher Strasse 47, D 50674 Cologne, Germany
J Biol Chem 282:34869-76. 2007..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...
- Defects in Protein Folding Machinery Affect Cell Wall Integrity and Reduce Ethanol Tolerance in S. cerevisiaeAswathy Narayanan
Molecular Genetics Laboratory, School of Biotechnology, National Institute of Technology Calicut, Calicut, Kerala, 673601, India
Curr Microbiol 73:38-45. 2016..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 ..
- Mistargeted mitochondrial proteins activate a proteostatic response in the cytosolLidia Wrobel
International Institute of Molecular and Cell Biology, 02 109 Warsaw, Poland
Nature 524:485-8. 2015..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. ..
- Cytosolic Hsp60 can modulate proteasome activity in yeastBella Kalderon
From the Department of Microbiology Molecular Genetics, IMRIC, Faculty of Medicine, Hebrew University of Jerusalem, Jerusalem 91120, Israel and
J Biol Chem 290:3542-51. 2015..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...
- Conformational switching of the 26S proteasome enables substrate degradationMary E Matyskiela
Department of Molecular and Cell Biology, University of California, Berkeley, California, USA
Nat Struct Mol Biol 20:781-8. 2013..Notably, Rpn11 moves from an occluded position to directly above the central pore, thus facilitating substrate deubiquitination concomitant with translocation. ..
- Crystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomesHideki Yashiroda
Laboratory of Frontier Science, Core Technology and Research Center, Tokyo Metropolitan Institute of Medical Science, Bunkyo ku, Tokyo 113 8613, Japan
Nat Struct Mol Biol 15:228-36. 2008..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...
- Hsm3/S5b participates in the assembly pathway of the 19S regulatory particle of the proteasomeBenoît Le Tallec
Laboratoire du Métabolisme de l ADN et Réponses aux Génotoxiques, SBIGeM, CEA, iBiTecS, Gif sur Yvette, F 91191, France
Mol Cell 33:389-99. 2009..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...
- Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitinationJames M Baugh
Department of Microbiology, University of Chicago, Chicago, IL 60637, USA
J Mol Biol 386:814-27. 2009..Collectively, these findings suggest a significant contribution of the ubiquitin-independent proteasome degradation pathway to the regulation of protein homeostasis in eukaryotes...
- Ribosome association and stability of the nascent polypeptide-associated complex is dependent upon its own ubiquitinationOlesya O Panasenko
Swiss Institute for Bioinformatics, University of Geneva, 1211 Geneva 4, Switzerland
Genetics 181:447-60. 2009..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...
- Substrate selection by the proteasome during degradation of protein complexesSumit Prakash
Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, 2205 Tech Drive, Evanston, Illinois 60208, USA
Nat Chem Biol 5:29-36. 2009..In addition, our data provide a plausible explanation for how adaptor proteins can bind to otherwise stable proteins and target them for degradation...
- The central unit within the 19S regulatory particle of the proteasomeRina Rosenzweig
Department of Biology, Technion Israel Institute of Technology, 32000 Haifa, Israel
Nat Struct Mol Biol 15:573-80. 2008..Similar pairing of units is found in unfoldases and nuclear transporters, exposing common features of these protein nanomachines...
- Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasomeGustavo M Silva
Instituto Butantan, Laboratorio de Bioquimica e Biofisica, Sao Paulo, Brazil, and Departamento de Genética e Biologia Evolutiva, Instituto de Biociencias, Universidade de Sao Paulo, Brazil
FEBS J 275:2942-55. 2008..These results indicate for the first time that 20S proteasome cysteinyl redox modification is a regulated mechanism coupled to enzymatic deglutathionylase activity...
- The suppressor gene scl1+ of Saccharomyces cerevisiae is essential for growthE Balzi
Unite de Biochimie Physiologique, Universite Catholique de Louvain, Louvain la Neuve, Belgium
Gene 83:271-9. 1989..The wild-type scl1+ gene was isolated by screening subclones of the 35-kb region between TRP5 and LEU1 for restoration of the ts ..
- A multimeric assembly factor controls the formation of alternative 20S proteasomesAndrew R Kusmierczyk
Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, Connecticut 06520 8114, USA
Nat Struct Mol Biol 15:237-44. 2008..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...
- Toward a general chemical method for rapidly mapping multi-protein complexesCarilee Denison
Center for Biomedical Inventions, Department of Internal Medicine, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd, Dallas, Texas 75390 8573, USA
J Proteome Res 3:417-25. 2004....
- 20 S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-glutathionylatedMarilene Demasi
Departmento de Biologia, Instituto de Biociencias, Universidade de Sao Paulo, Rua do Matao, 277 São Paulo, Sao Paulo 05508 900, Brazil
J Biol Chem 278:679-85. 2003..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...
- Cic1, an adaptor protein specifically linking the 26S proteasome to its substrate, the SCF component Cdc4S Jager
Institut für Biochemie der Universität Stuttgart, Pfaffenwaldring 55, D 70569 Stuttgart, Germany
EMBO J 20:4423-31. 2001..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...
- Subcellular distribution of proteasomes implicates a major location of protein degradation in the nuclear envelope-ER network in yeastC Enenkel
Institut fur Biochemie, Humboldt Universitat, Universitatsklinikum Charite, Monbijoustrasse 2, D 10117 Berlin, Germany
EMBO J 17:6144-54. 1998..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...
- Yeast cycloheximide-resistant crl mutants are proteasome mutants defective in protein degradationU M Gerlinger
Institut fur Biochemie, Universitat Stuttgart, Pfaffenwaldring 55, 70569 Stuttgart, Germany
Mol Biol Cell 8:2487-99. 1997..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...
- Cycloheximide-resistant temperature-sensitive lethal mutations of Saccharomyces cerevisiaeJ H McCusker
Department of Biology, Brandeis University, Waltham, Massachusetts 02254
Genetics 119:303-15. 1988..We also describe two new methods for the enrichment of auxotrophic mutations from a wild-type yeast strain...
- Reversible cytoplasmic localization of the proteasome in quiescent yeast cellsDamien Laporte
Institut de Biochimie et Génétique Cellulaires, Université Victor Segalen Bordeaux II, 33077 Bordeaux, France
J Cell Biol 181:737-45. 2008..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...
- The 26S proteasome: a molecular machine designed for controlled proteolysisD Voges
Max Planck Institut fur Biochemie, Martinsried, Germany
Annu Rev Biochem 68:1015-68. 1999..A low-resolution structure of the 26S proteasome has been obtained by electron microscopy, but the precise arrangement of subunits in the 19S complex is unclear...