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J. Biol. Chem., Vol. 282, Issue 47, 33902-33907, November 23, 2007

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HSF1-TPR Interaction Facilitates Export of Stress-induced HSP70 mRNA^*

From the Department of Molecular and Cellular Biochemistry, Chandler Medical Center, University of Kentucky, Lexington, Kentucky 40536-0084

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.

Received for publication, May 16, 2007 , and in revised form, September 25, 2007.

^* This work was supported by National Institutes of Health Grants GM61053 and GM64606 (to K. D. S.), Training Grant T32ES007266 (Department of Toxicology; to H. S. S.), and Postdoctoral Grant HD50043 (to D. C. W.). 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.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. S1.

This article was selected as a Paper of the Week.

¹ Present address: Div. of Hematology and Oncology, Markey Center, University of Kentucky, Lexington, KY 40536-0084.

² Present address: Dept. of Biology, University of Dayton, Dayton, OH 45469.

³ Present address: Dept. of Cell and Cancer Biology, University of Cincinnati, Cincinnati, OH 45267.

⁴ To whom correspondence should be addressed: Dept. of Molecular and Cellular Biochemistry, Chandler Medical Center, University of Kentucky, 741 S. Limestone St., Lexington, KY 40536-0084. Tel.: 859-323-5777; Fax: 859-323-1037; E-mail: kdsarge{at}uky.edu.

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