HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 277, Issue 18, 15586-15591, May 3, 2002

This Article Full Text Full Text (PDF) All Versions of this Article: 277/18/15586    most recent M200800200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Hyman, L. E. Articles by Baricos, W. H. Search for Related Content PubMed PubMed Citation Articles by Hyman, L. E. Articles by Baricos, W. H. Social Bookmarking                      What's this?

Binding to Elongin C Inhibits Degradation of Interacting Proteins in Yeast^*

Linda E. Hyman, Edward Kwon, Sumana Ghosh, Jennifer McGee, Anna M. Boguszewska Chachulska^§, Tanya Jackson, and William H. Baricos

From the Department of Biochemistry, Tulane University Health Science Center, New Orleans, Louisiana 70112

Elongin C is a highly conserved, low molecular weight protein found in a variety of multiprotein complexes in human, rat, fly, worm, and yeast cells. Among the best characterized of these complexes is a mammalian E3 ligase that targets proteins for ubiquitination and subsequent degradation by the 26 S proteasome. Despite its crucial role as a component of such E3 ligases and other complexes, the specific function of Elongin C is unknown. In yeast, Elongin C is a non-essential gene and there is no obvious phenotype as associated with its absence. We previously reported that in Saccharomyces cerevisiae Elongin C (Elc1) interacts specifically and strongly with a class of proteins loosely defined as stress response proteins. In the present study, we examined the role of yeast Elc1 in the turnover of two of these binding partners, Snf4 and Pcl6. Deletion of Elc1 resulted in decreased steady-state levels of Snf4 and Pcl6 as indicated by Western blot analysis. Northern blot analysis of mRNA prepared from elc1 null and wild type strains revealed no difference in mRNA levels for Snf4 and Pcl6 establishing that the effects of Elc1 are not transcriptionally mediated. Reintroduction of either yeast or human Elongin C into Elc1 null strains abrogated this effect. Taken together, these data document that the levels of Snf4 and Pcl6 are dependent on the presence of Elc1 and that binding to Elc1 inhibits the degradation of these proteins. The results suggest a new function for yeast Elongin C that is distinct from a direct role in targeting proteins for ubiquitination and subsequent proteolysis.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				M. Momcilovic, S. H. Iram, Y. Liu, and M. Carlson Roles of the Glycogen-binding Domain and Snf4 in Glucose Inhibition of SNF1 Protein Kinase J. Biol. Chem., July 11, 2008; 283(28): 19521 - 19529. [Abstract] [Full Text] [PDF]

				K. L. Ramsey, J. J. Smith, A. Dasgupta, N. Maqani, P. Grant, and D. T. Auble The NEF4 Complex Regulates Rad4 Levels and Utilizes Snf2/Swi2-Related ATPase Activity for Nucleotide Excision Repair Mol. Cell. Biol., July 15, 2004; 24(14): 6362 - 6378. [Abstract] [Full Text] [PDF]