JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/jbc.M407264200 on October 22, 2004

J. Biol. Chem., Vol. 279, Issue 53, 55425-55432, December 31, 2004
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
279/53/55425    most recent
M407264200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Durchschlag, E.
Right arrow Articles by Schüller, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Durchschlag, E.
Right arrow Articles by Schüller, C.
Related Collections
Right arrow Papers Of The Week
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Nuclear Localization Destabilizes the Stress-regulated Transcription Factor Msn2*{diamondsuit}

Erich Durchschlag{ddagger}§, Wolfgang Reiter{ddagger}, Gustav Ammerer, and Christoph Schüller¶

From the Institute of Biochemistry and Molecular Cell Biology and Ludwig Boltzmann Forschungsstelle for Biochemistry, Max F. Perutz Laboratories, University and BioCenter of Vienna, A-1030 Vienna, Austria

The transcriptional program of yeast cells undergoes dramatic changes during the shift from fermentative growth to respiratory growth. A large part of this response is mediated by the stress responsive transcription factor Msn2. During glucose exhaustion, Msn2 is activated and concentrated in the nucleus. Simultaneously, Msn2 protein levels also drop significantly under this condition. Here we show that the decrease in Msn2 concentration is due to its increased degradation. Moreover, Msn2 levels are also reduced under chronic stress or low protein kinase A (PKA) activity, both conditions that cause a predominant nuclear localization of Msn2. Similar effects were found in msn5 mutant cells that block Msn2 nuclear export. To approximate the effect of low PKA activity on Msn2, we generated a mutant form with alanine substitutions in PKA phosphorylation sites. High expression of this Msn2 mutant is detrimental for growth, suggesting that the increased degradation of nuclear Msn2 might be necessary to adapt cells to low PKA conditions after the diauxic shift or to allow growth under chronic stress conditions.


Received for publication, June 29, 2004 , and in revised form, October 13, 2004.

* This work was supported by Austrian Science Fund (FWF) Grants P12015, P13493, and P14653 (to G. A. and the late H. Ruis). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

{diamondsuit} This article was selected as a Paper of the Week.

{ddagger} These authors contributed equally to this work.

§ Current address: Ludwig Baltzmann Institute of Osteology at the Hanusch Hospital of WGKK and AUVA Trauma Centre, Meidling 4th Medical Dept., Hanusch Hospital, Heinrich Collin Str. 30, A-1140, Vienna.

To whom correspondence and reprint requests should be addressed: Inst. of Biochemistry and Molecular Cell Biology, Max F. Perutz Laboratories, University and BioCenter of Vienna, Dr. Bohr-Gasse 9/5, A-1030 Vienna, Austria. Tel.: 43-1-4277-52815; Fax: 43-1-4277-9528; E-mail: Christoph.Schueller{at}univie.ac.at.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Eukaryot CellHome page
A. Demczuk, N. Guha, P. H. Nguyen, P. Desai, J. Chang, K. Guzinska, J. Rollins, C. C. Ghosh, L. Goodwin, and A. Vancura
Saccharomyces cerevisiae Phospholipase C Regulates Transcription of Msn2p-Dependent Stress-Responsive Genes
Eukaryot. Cell, June 1, 2008; 7(6): 967 - 979.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
C. Li, R.-C. Wu, L. Amazit, S. Y. Tsai, M.-J. Tsai, and B. W. O'Malley
Specific Amino Acid Residues in the Basic Helix-Loop-Helix Domain of SRC-3 Are Essential for Its Nuclear Localization and Proteasome-Dependent Turnover
Mol. Cell. Biol., February 15, 2007; 27(4): 1296 - 1308.
[Abstract] [Full Text] [PDF]


Home page
Microbiol. Mol. Biol. Rev.Home page
G. M. Santangelo
Glucose Signaling in Saccharomyces cerevisiae
Microbiol. Mol. Biol. Rev., March 1, 2006; 70(1): 253 - 282.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2004 by the American Society for Biochemistry and Molecular Biology.