Genomes and Genes
Gene Symbol: RPN8
Description: proteasome regulatory particle lid subunit RPN8
Species: Saccharomyces cerevisiae S288c
- Sem1p is a novel subunit of the 26 S proteasome from Saccharomyces cerevisiaeTakayuki Sone
Department of Biochemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060 0812, Japan
J Biol Chem 279:28807-16. 2004..The results suggest that Sem1, possibly hDSS1, is a novel subunit of the 26 S proteasome and plays a role in ubiquitin-dependent proteolysis...
- Complete subunit architecture of the proteasome regulatory particleGabriel C Lander
Life Sciences Division, Lawrence Berkeley National Laboratory, University of California, Berkeley, California 94720, USA
Nature 482:186-91. 2012..We provide a structural basis for the ability of the proteasome to degrade a diverse set of substrates and thus regulate vital cellular processes...
- Rpn7 Is required for the structural integrity of the 26 S proteasome of Saccharomyces cerevisiaeErika Isono
Department of Biological Sciences, Graduate School of Science, University of Tokyo, Hongo, Tokyo 113 0033, Japan
J Biol Chem 279:27168-76. 2004..From these results, we concluded that Rpn7 is required for the integrity of the 26 S complex by establishing a correct lid structure...
- N-Terminal modifications of the 19S regulatory particle subunits of the yeast proteasomeYayoi Kimura
Kihara Institute for Biological Research Graduate School of Integrated Science, Yokohama City University, Maioka 641 12, Totsuka, Yokohama, Japan
Arch Biochem Biophys 409:341-8. 2003..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 substrates...
- The regulatory particle of the Saccharomyces cerevisiae proteasomeM H Glickman
Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA
Mol Cell Biol 18:3149-62. 1998..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...
- Atomic structure of the 26S proteasome lid reveals the mechanism of deubiquitinase inhibitionCorey M Dambacher
Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, United States
elife 5:e13027. 2016....
- The Proteasome Subunit Rpn8 Interacts with the Small Nucleolar RNA Protein (snoRNP) Assembly Protein Pih1 and Mediates Its Ubiquitin-independent Degradation in Saccharomyces cerevisiaeAlexandr Paci
From the Department of Biological Sciences, University of Toronto, Toronto, Ontario M1C 1A4, Canada
J Biol Chem 291:11761-75. 2016..we investigated Pih1 interactors and identified a specific interaction between Pih1 and the proteasome subunit Rpn8 in yeast Saccharomyces cerevisiae when HSP90 co-chaperone Tah1 is depleted...
- A Single α Helix Drives Extensive Remodeling of the Proteasome Lid and Completion of Regulatory Particle AssemblyRobert J Tomko
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520 8114, USA Electronic address
Cell 163:432-44. 2015..Such assembly-coupled conformational switching is reminiscent of viral particle maturation and may represent a commonly used mechanism to enforce hierarchical assembly in multisubunit complexes...
- Solution Structure of the Cuz1 AN1 Zinc Finger Domain: An Exposed LDFLP Motif Defines a Subfamily of AN1 ProteinsZhen Yu J Sun
Department of Biological Chemistry and Molecular Physiology, Harvard Medical School, Boston, Massachusetts, United States of America
PLoS ONE 11:e0163660. 2016..These results provide the first structural characterization of the AN1 zinc finger domain, and suggest that the LDFLP motif may define a sub-family of evolutionarily conserved AN1 zinc finger proteins...
- High-resolution cryo-EM structure of the proteasome in complex with ADP-AlFxZhanyu Ding
National Center for Protein Science Shanghai, State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences University of Chinese Academy of Sciences, 333 Haike Road, Shanghai 201203, China
Cell Res . 2017..Cell Research advance online publication 20 January 2017; doi:10.1038/cr.2017.12...
- Base-CP proteasome can serve as a platform for stepwise lid formationZanlin Yu
Department of Biology, Technion Israel Institute of Technology, 32000 Haifa, Israel
Biosci Rep 35:. 2015..Even within the lid, subunits have been demarcated into two modules: module 1 (Rpn5, Rpn6, Rpn8, Rpn9 and Rpn11), which interacts with both CP and base sub-complexes and module 2 (Rpn3, Rpn7, Rpn12 and Rpn15) ..
- The protein quality control machinery regulates its misassembled proteasome subunitsLee Zeev Peters
Faculty of life sciences Bar Ilan University, Ramat Gan, Israel
PLoS Genet 11:e1005178. 2015..Thus, we show that proteasome homeostasis is controlled through probing the level of proteasome assembly, and the interplay between UPS mediated degradation or their sorting into distinct cellular compartments. ..
- Disassembly of Lys11 and mixed linkage polyubiquitin conjugates provides insights into function of proteasomal deubiquitinases Rpn11 and Ubp6Wissam Mansour
From the Department of Biology, Technion Israel Institute of Technology, 32000 Haifa, Israel
J Biol Chem 290:4688-704. 2015..The reduced ability to disassemble homogeneous Lys(48)-linked chains longer than 4 Ub units may prolong residency time on the proteasome. ..
- Crystal structure of the proteasomal deubiquitylation module Rpn8-Rpn11Ganesh Ramnath Pathare
Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany
Proc Natl Acad Sci U S A 111:2984-9. 2014..Here we describe three crystal structures of the heterodimer of the Mpr1-Pad1-N-terminal domains of Rpn8 and Rpn11, crystallized as a fusion protein in complex with a nanobody...
- Structure of the Rpn11-Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradationEvan J Worden
Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California, USA
Nat Struct Mol Biol 21:220-7. 2014..crystal structures of Zn(2+)-free and Zn(2+)-bound Saccharomyces cerevisiae Rpn11 in an MPN-domain heterodimer with Rpn8. The Rpn11-Rpn8 interaction occurs via two distinct interfaces that may be conserved in related MPN-domain ..
- The intrinsically disordered Sem1 protein functions as a molecular tether during proteasome lid biogenesisRobert J Tomko
Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520 8114, USA
Mol Cell 53:433-43. 2014..Thus, although Sem1 is a stoichiometric component of the mature proteasome, it has a distinct, chaperone-like function specific to early stages of proteasome assembly...
- Formation of an intricate helical bundle dictates the assembly of the 26S proteasome lidEric Estrin
Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA
Structure 21:1624-35. 2013..Finally, we predict that the assembly of the COP9 signalosome depends on a similar helical bundle...
- Proteasome-mediated degradation of cotranslationally damaged proteins involves translation elongation factor 1AShow Mei Chuang
Department of Biochemistry, Robert Wood Johnson Medical School, 683 Hoes Lane, Piscataway, NJ 08854, USA
Mol Cell Biol 25:403-13. 2005..Our findings provide a mechanistic foundation for defining how cellular proteins are degraded cotranslationally...
- Preparation of ubiquitinated substrates by the PY motif-insertion method for monitoring 26S proteasome activityY Saeki
Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan
Methods Enzymol 399:215-27. 2005..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...
- Incorporation of the Rpn12 subunit couples completion of proteasome regulatory particle lid assembly to lid-base joiningRobert J Tomko
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520 8114, USA
Mol Cell 44:907-17. 2011..Rpn12 incorporation thus links proper lid assembly to subsequent assembly steps...
- Ubiquitin-dependent protein degradationM Hochstrasser
Department of Biochemistry and Molecular Biology, University of Chicago, Illinois 60637, USA
Annu Rev Genet 30:405-39. 1996..This diversity underlies both the high substrate specificity of the ubiquitin system and the variety of regulatory mechanisms that it serves...
- 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. ..
- Similar temporal and spatial recruitment of native 19S and 20S proteasome subunits to transcriptionally active chromatinFuqiang Geng
Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, 465 21st Avenue South, Nashville, TN 37232, USA
Proc Natl Acad Sci U S A 109:6060-5. 2012..We find that proteasome subunits Rpt1, Rpt4, Rpn8, Rpn12, Pre6, and Pre10 are recruited to GAL10 rapidly upon galactose induction...
- Leucyl-tRNA synthetase controls TORC1 via the EGO complexGrégory Bonfils
Department of Biology, Division of Biochemistry, University of Fribourg, CH 1700 Fribourg, Switzerland
Mol Cell 46:105-10. 2012..Thus, the EGOC-TORC1 signaling module samples, via the LeuRS-intrinsic editing domain, the fidelity of tRNA(Leu) aminoacylation as a proxy for leucine availability...
- Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle baseMinoru Funakoshi
Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520 8114, USA
Cell 137:887-99. 2009..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...
- 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...
- Subunit architecture of intact protein complexes from mass spectrometry and homology modelingThomas Taverner
Department of Chemistry, Lensfield Road, University of Cambridge, Cambridge CB2 1EW, UK
Acc Chem Res 41:617-27. 2008..Overall therefore this mass spectrometry and homology modeling approach has given significant insight into the structure of two previously intractable protein complexes and as such has broad application in structural biology...
- tRNA import into yeast mitochondria is regulated by the ubiquitin-proteasome systemIrina Brandina
Unité Mixte de Recherche 7156 GMGM, Department of Molecular and Cellular Genetics, Centre National de la Recherche Scientifique ULP, 21 rue René Descartes, Strasbourg 67084, France
FEBS Lett 581:4248-54. 2007..This result suggests a functional link between UPS and tRNA mitochondrial import in yeast and indicates on the existence of negative and positive import regulators...
- Structural organization of the 19S proteasome lid: insights from MS of intact complexesMichal Sharon
Department of Chemistry, University of Cambridge, Cambridge, United Kingdom
PLoS Biol 4:e267. 2006..More generally, the results highlight the potential of mass spectrometry to add crucial insight into the structural organization of an endogenous, wild-type complex...
- Multiple proteasome-interacting proteins assist the assembly of the yeast 19S regulatory particleYasushi Saeki
Laboratory of Frontier Science, Core Technology and Research Center, Tokyo Metropolitan Institute of Medical Science, 2 1 6 Kamikitazawa, Setagaya Ku, Tokyo 156 8506, Japan
Cell 137:900-13. 2009..Our results indicate that the RP assembly is a highly organized and elaborate process orchestrated by multiple proteasome-dedicated chaperones...
- Participation of the proteasomal lid subunit Rpn11 in mitochondrial morphology and function is mapped to a distinct C-terminal domainTeresa Rinaldi
Pasteur Institute Cenci Bolognetti Foundation and the Department of Cell and Developmental Biology, University of Rome I, 00185 Rome, Italy
Biochem J 381:275-85. 2004..We find that overexpression of WT (wild-type) RPN8, encoding a paralogous subunit that does not contain the catalytic MPN+ motif, corrects proteasome conformations ..
- Evidence for an interaction between ubiquitin-conjugating enzymes and the 26S proteasomeP Tongaonkar
Department of Biochemistry, Robert Wood Johnson Medical School UMDNJ, Piscataway, NJ 08854, USA
Mol Cell Biol 20:4691-8. 2000..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...
- Recovery from DNA replicational stress is the essential function of the S-phase checkpoint pathwayB A Desany
Verna and Marrs McLean Department of Biochemistry, Howard Hughes Medical Institute, Baylor College of Medicine, Houston, Texas 77030 USA
Genes Dev 12:2956-70. 1998..We propose that this checkpoint pathway plays an important role in the maintenance of DNA synthetic capabilities when DNA replication is stressed...
- Unified nomenclature for subunits of the Saccharomyces cerevisiae proteasome regulatory particleD Finley
Trends Biochem Sci 23:244-5. 1998
- Synthetic lethality of rpn11-1 rpn10Δ is linked to altered proteasome assembly and activityAbhishek Chandra
Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA
Curr Genet 56:543-57. 2010..Based on these findings, we propose that the lethality of rpn11-1 rpn10Δ results primarily from altered proteasome integrity. It is conceivable that Rpn10/Rpn11 interaction couples proteasome assembly to substrate binding...