Sumo-1 modification regulates the DNA binding activity of heat shock transcription factor 2, a promyelocytic leukemia nuclear body associated transcription factor.

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.
Mesh Terms:
Biological Transport, DNA, DNA-Binding Proteins, Gene Expression Regulation, Heat-Shock Proteins, Hela Cells, Humans, Protein Binding, SUMO-1 Protein, Saccharomyces cerevisiae, Transcription Factors, Ubiquitins
J. Biol. Chem.
Date: May. 25, 2001
Download Curated Data For This Publication
4011
Switch View:
  • Interactions 1