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

J. Biol. Chem., Vol. 279, Issue 27, 28174-28181, July 2, 2004

This Article Full Text Full Text (PDF) All Versions of this Article: 279/27/28174    most recent M401595200v1 Alert me when this article is cited 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 Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Betz, C. Articles by Bailer, S. M. Search for Related Content PubMed PubMed Citation Articles by Betz, C. Articles by Bailer, S. M. Social Bookmarking                      What's this?

Asr1p, a Novel Yeast Ring/PHD Finger Protein, Signals Alcohol Stress to the Nucleus^*

Christian Betz, Gabriel Schlenstedt, and Susanne M. Bailer

From the Universität des Saarlandes, Medizinische Biochemie und Molekularbiologie, Gebäude 44, D-66421 Homburg/Saar, Germany

During fermentation, yeast cells are exposed to increasing amounts of alcohol, which is stressful and affects both growth and viability. On the molecular level, numerous aspects of alcohol stress signaling remain unresolved. We have identified a novel yeast Ring/PHD finger protein that constitutively shuttles between nucleus and cytoplasm but accumulates in the nucleus upon exposure to ethanol, 2-propanol, or 1-butanol. Subcellular localization of this protein is not altered by osmotic, oxidative, or heat stress or during nitrogen or glucose starvation. Because of its exclusive sensitivity to environmental alcohol, the protein was called Asr1p for Alcohol Sensitive Ring/PHD finger 1 protein. Nuclear accumulation of Asr1p is rapid, reversible, and requires a functional Ran/Gsp1p gradient. Asr1p contains two N terminally located leucine-rich nuclear export sequences (NES) required for nuclear export. Consistently, it accumulates in the nucleus of xpo1-1 cells at restrictive temperature and forms a trimeric complex with the exportin Xpo1p and Ran-GTP. Deletion of ASR1 leads to sensitivity in growth on medium containing alcohol or detergent, consistent with a function of Asr1p in alcohol-related signaling. Asr1p is the first reported protein that changes its subcellular localization specifically upon exposure to alcohol and therefore represents a key element in the analysis of alcohol-responsive signaling.

Received for publication, February 13, 2004 , and in revised form, April 21, 2004.

^* 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.

To whom correspondence should be addressed. Tel.: 49-06841-162-6523 (laboratory), 49-06841-162-6046 (office); Fax: 49-06841-162-6027; E-mail: dr.susanne.bailer{at}med-rz.uni-saarland.de.

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

This article has been cited by other articles:

				P. A. Gibney, T. Fries, S. M. Bailer, and K. A. Morano Rtr1 Is the Saccharomyces cerevisiae Homolog of a Novel Family of RNA Polymerase II-Binding Proteins Eukaryot. Cell, June 1, 2008; 7(6): 938 - 948. [Abstract] [Full Text] [PDF]

				T. Fries, C. Betz, K. Sohn, S. Caesar, G. Schlenstedt, and S. M. Bailer A Novel Conserved Nuclear Localization Signal Is Recognized by a Group of Yeast Importins J. Biol. Chem., July 6, 2007; 282(27): 19292 - 19301. [Abstract] [Full Text] [PDF]