Document Detail

Genetic dissection of the yeast 26S proteasome: cell cycle defects caused by the Deltarpn9 mutation.
MedLine Citation:
PMID:  11295494     Owner:  NLM     Status:  MEDLINE    
Rpn9 is one of the subunits of the regulatory particle of the yeast 26S proteasome and is needed for stability or efficient assembly of the 26S proteasome. As anticipated from the fact that the rpn9 disruptant grew at 25 degrees C but arrested in G2/M phase at 37 degrees C, the CDK inhibitor Sic1p was found to be degraded at the G1/S boundary in the Deltarpn9 cells. The degradation of the anaphase inhibitor Pds1p was delayed in the Deltarpn9 cells. Clb2p in M phase, as well as that ectopically expressed in G1 and S phases, was degraded more slowly in the Deltarpn9 cells than in the wild type cells, indicating that the 26S proteasome lacking Rpn9 uses Sic1p as a better substrate than Pds1p and Clb2p. These results, in addition to the fact that multiubiquitinated proteins were accumulated in the Deltarpn9 cells incubated at 37 degrees C, strongly suggest that Rpn9 is involved in the proteolysis of a subset of the substrates degraded by the 26S proteasome. The Deltarpn9 Deltapds1 double mutant was unable to elongate spindle at a restrictive temperature, suggesting that some protein(s) other than Scc1 (cohesin) should be degraded during progression of anaphase.
J Takeuchi; A Toh-e
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochimie     Volume:  83     ISSN:  0300-9084     ISO Abbreviation:  Biochimie     Publication Date:    2001 Mar-Apr
Date Detail:
Created Date:  2001-04-11     Completed Date:  2001-06-14     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  1264604     Medline TA:  Biochimie     Country:  France    
Other Details:
Languages:  eng     Pagination:  333-40     Citation Subset:  IM    
Department of Biological Sciences, Graduate School of Science, University of Tokyo, Hongo, 113-0033, Tokyo, Japan.
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MeSH Terms
Anaphase / genetics*,  physiology
Cell Cycle / genetics
Cell Cycle Proteins / genetics,  metabolism
Gene Deletion
Mitosis / genetics*,  physiology
Mitotic Spindle Apparatus / genetics*,  metabolism
Multienzyme Complexes / genetics*,  metabolism
Mutation / genetics
Peptide Hydrolases / genetics*,  metabolism
Proteasome Endopeptidase Complex*
Protein Subunits
Saccharomyces cerevisiae / cytology,  genetics*,  metabolism
Ubiquitins / metabolism
Reg. No./Substance:
0/Cell Cycle Proteins; 0/Multienzyme Complexes; 0/Protein Subunits; 0/Ubiquitins; EC 3.4.-/Peptide Hydrolases; EC Endopeptidase Complex; EC 3.4.99.-/ATP dependent 26S protease

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