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Originally published In Press as doi:10.1074/jbc.M008066200 on February 15, 2001

J. Biol. Chem., Vol. 276, Issue 21, 18513-18518, May 25, 2001
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SUMO-1 Modification Regulates the DNA Binding Activity of Heat Shock Transcription Factor 2, a Promyelocytic Leukemia Nuclear Body Associated Transcription Factor*

Michael L. GoodsonDagger §, Yiling HongDagger §, Richard Rogers, Michael J. Matunis, Ok-Kyong Park-Sarge||, and Kevin D. SargeDagger **

From the Dagger  Department of Molecular and Cellular Biochemistry and || Department of Physiology, Chandler Medical Center, University of Kentucky, Lexington, Kentucky 405036-0298, and the  Department of Biochemistry and Molecular Biology, School of Hygiene and Public Health, Johns Hopkins University, Baltimore, Maryland 21205

Heat shock transcription factor 2 (HSF2) is a transcription factor that regulates heat shock protein gene expression, but the mechanisms regulating the function of this factor are unclear. Here we report that HSF2 is a substrate for modification by the ubiquitin-related protein SUMO-1 and that HSF2 colocalizes in cells with SUMO-1 in nuclear granules. Staining with anti-promyelocytic leukemia antibodies indicates that these HSF2-containing nuclear granules are PML bodies. Our results identify lysine 82 as the major site of SUMO-1 modification in HSF2, which is located in a "wing" within the DNA-binding domain of this protein. Interestingly, SUMO-1 modification of HSF2 results in conversion of this factor to the active DNA binding form. This is the first demonstration that SUMO-1 modification can directly alter the DNA binding ability of a transcription factor and reveals a new mechanism by which SUMO-1 modification can regulate protein function.

* This work was supported by National Institutes of Health Grant HD32008 and American Cancer Society Grant RPG 99-217 (to K. D. S.) and National Institutes of Health Training Grant ES 07266 postdoctoral support (to Y. H.).

§ These authors contributed equally to this work.

** To whom correspondence should be addressed. Department of Biochemistry, University of Kentucky, 800 Rose Street, Lexington, KY 40536. Tel.: 859-323-5777; Fax: 859-323-1037; E-mail: kdsarge@pop.uky.edu

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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