- THIS ARTICLE
- Full Text (Rapid PDF)
-
All Versions of this Article:
genetics.105.046888v1
171/4/1477 most recent - Alert me when this article is cited
- Alert me if a correction is posted
- SERVICES
- Similar articles in this journal
- Similar articles in PubMed
- Alert me to new issues of the journal
- Download to citation manager
- Reprints & Permissions
- CITING ARTICLES
- Citing Articles via HighWire
- Citing Articles via Google Scholar
- GOOGLE SCHOLAR
- Articles by Chuang, S.-M.
- Articles by Madura, K.
- Search for Related Content
- PUBMED
- PubMed Citation
- Articles by Chuang, S.-M.
- Articles by Madura, K.
doi:10.1534/genetics.105.046888
A more recent version of this article appeared on December 1, 2005.
REGULAR RESEARCH PAPERS |
Saccharomyces cerevisiae Ub-conjugating enzyme Ubc4 binds the proteasome in the presence of translationally-damaged proteins
Show-Mei Chuang 1 and Kiran Madura 2*
1 Robert Wood Johnson Medical School
2 UMDNJ
* To whom correspondence should be addressed. E-mail: maduraki{at}umdnj.edu.
Submitted on June 14, 2005
Revised on July 14, 2005
Accepted on 3 August 2005
Surveillance mechanisms that monitor protein synthesis can promote rapid elimination of misfolded nascent proteins. We showed that the translation elongation factor eEF1A and the proteasome subunit Rpt1 play a central role in the translocation of nascent damaged proteins to the proteasome. We show here that multi-ubiquitinated proteins, and the ubiquitin-conjugating enzyme Ubc4, are rapidly detected in the proteasome following translational damage. However, Ubc4 levels in the proteasome were reduced significantly in a strain that expressed a mutant Rpt1 subunit. Ubc4 is an ideal candidate for ubiquitinating damaged nascent proteins, because it lacks significant substrate specificity, is required for the degradation of bulk, damaged proteins, and contributes to cellular stress-tolerance mechanisms. In agreement with this hypothesis, we determined that ubc4D ubc5D is exceedingly sensitive to protein translation inhibitors. Moreover, a nascently damaged test protein accumulated in proteasomes purified from ubc4D, suggesting a specific role for Ubc4/5 in the degradation of cotranslationally damaged proteins that are targeted to the proteasome.
Key Words: Ubc4, co-translational degradation, eEF1A, proteasome, ubiquitin
This article has been cited by other articles:
 |
|
 |
|
  D. A. Dalmas, M. S. Scicchitano, Y. Chen, J. Kane, R. Mirabile, L. W. Schwartz, H. C. Thomas, and R. W. Boyce Transcriptional Profiling of Laser Capture Microdissected Rat Arterial Elements: Fenoldopam-induced Vascular Toxicity as a Model System Toxicol Pathol, April 1, 2008; 36(3): 496 - 519. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K. W. Mulder, A. Inagaki, E. Cameroni, F. Mousson, G. S. Winkler, C. De Virgilio, M. A. Collart, and H. Th. M. Timmers Modulation of Ubc4p/Ubc5p-Mediated Stress Responses by the RING-Finger-Dependent Ubiquitin-Protein Ligase Not4p in Saccharomyces cerevisiae Genetics, May 1, 2007; 176(1): 181 - 192. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 O. Panasenko, E. Landrieux, M. Feuermann, A. Finka, N. Paquet, and M. A. Collart The Yeast Ccr4-Not Complex Controls Ubiquitination of the Nascent-associated Polypeptide (NAC-EGD) Complex J. Biol. Chem., October 20, 2006; 281(42): 31389 - 31398. [Abstract] [Full Text] [PDF]
|
|