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Papers In Press, published online ahead of print February 15, 2001
Biochemistry, University of Kentucky, Lexington, KY 40536
Corresponding Author: kdsarge{at}pop.uky.edu
HSF2 is a transcription factor that regulates hsp 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-PML 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.
J. Biol. Chem, 10.1074/jbc.M008066200
Submitted on September 4, 2000
Revised on February 1, 2001
Accepted on February 15, 2001
SUMO-1 modification regulates the DNA-binding activity of heat shock transcription factor 2 (HSF2), a PML nuclear body associated transcription factor
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