JBC Anatrace, Inc.

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on November 23, 2007
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow Supplemental Data
Right arrow All Versions of this Article:
282/47/33902    most recent
M704054200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
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 Skaggs, H. S.
Right arrow Articles by Sarge, K. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Skaggs, H. S.
Right arrow Articles by Sarge, K. D.
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?

Papers In Press, published online ahead of print September 25, 2007
J. Biol. Chem, 10.1074/jbc.M704054200
Submitted on May 16, 2007
Revised on September 25, 2007
Accepted on September 25, 2007

HSF1-Tpr interaction facilitates export of stress-induced hsp70 mRNA

Hollie S. Skaggs, Hongyan Xing, Donald C. Wilkerson, Lynea A. Murphy, Yiling Hong, Christopher N. Mayhew, and Kevin D. Sarge

Department of Biochemistry, University of Kentucky Medical Center, Lexington, KY 40536-0084

Corresponding Author: kdsarge{at}uky.edu

Stress conditions inhibit mRNA export, but mRNAs encoding heat shock proteins continue to be efficiently exported from the nucleus during stress. How hsp mRNAs bypass this stress-associated export inhibition was not known. Here we show that HSF1, the transcription factor that binds hsp promoters after stress to induce their transcription, interacts with the nuclear pore-associating Tpr protein in a stress-responsive manner. Tpr is brought into proximity of the hsp70 promoter after stress and preferentially associates with mRNAs transcribed from this promoter. Disruption of the HSF1-Tpr interaction inhibits the export of mRNAs expressed from the hsp70 promoter, both endogenous hsp70 mRNA and a luciferase reporter mRNA. These results suggest that hsp mRNA export escapes stress inhibition via HSF1-mediated recruitment of the nuclear pore-associating protein Tpr to hsp genes, thereby functionally connecting the first and last nuclear steps of the gene expression pathway, transcription and mRNA export.


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
 Mol. Cell. Biol.Home page
T.-C. Lu, Z. Wang, X. Feng, P. Chuang, W. Fang, Y. Chen, S. Neves, A. Maayan, H. Xiong, Y. Liu, et al.
Retinoic Acid Utilizes CREB and USF1 in a Transcriptional Feed-Forward Loop in Order To Stimulate MKP1 Expression in Human Immunodeficiency Virus-Infected Podocytes
Mol. Cell. Biol., September 15, 2008; 28(18): 5785 - 5794.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2007 by the American Society for Biochemistry and Molecular Biology.