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Inhibition of DNA Binding by Differential Sumoylation of Heat Shock Factors
- Source :
- Molecular and Cellular Biology. 26:955-964
- Publication Year :
- 2006
- Publisher :
- Informa UK Limited, 2006.
-
Abstract
- Covalent modification of proteins by the small ubiquitin-related modifier SUMO regulates diverse biological functions. Sumoylation usually requires a consensus tetrapeptide, through which the binding of the SUMO-conjugating enzyme Ubc9 to the target protein is directed. However, additional specificity determinants are in many cases required. To gain insights into SUMO substrate selection, we have utilized the differential sumoylation of highly similar loop structures within the DNA-binding domains of heat shock transcription factor 1 (HSF1) and HSF2. Site-specific mutagenesis in combination with molecular modeling revealed that the sumoylation specificity is determined by several amino acids near the consensus site, which are likely to present the SUMO consensus motif to Ubc9. Importantly, we also demonstrate that sumoylation of the HSF2 loop impedes HSF2 DNA-binding activity, without affecting its oligomerization. Hence, SUMO modification of the HSF2 loop contributes to HSF-specific regulation of DNA binding and broadens the concept of sumoylation in the negative regulation of gene expression.
- Subjects :
- Consensus site
Molecular Sequence Data
SUMO protein
SUMO enzymes
Biology
Ubiquitin-conjugating enzyme
Transfection
Mice
Heat Shock Transcription Factors
Heat shock protein
Chlorocebus aethiops
Animals
Humans
Amino Acid Sequence
HSF1
Molecular Biology
Transcription factor
Conserved Sequence
Heat-Shock Proteins
Genetics
Articles
DNA
Cell Biology
Cell biology
DNA-Binding Proteins
Heat shock factor
COS Cells
Ubiquitin-Conjugating Enzymes
Small Ubiquitin-Related Modifier Proteins
Protein Processing, Post-Translational
Transcription Factors
Subjects
Details
- ISSN :
- 10985549
- Volume :
- 26
- Database :
- OpenAIRE
- Journal :
- Molecular and Cellular Biology
- Accession number :
- edsair.doi.dedup.....b9f9bd1acdb8599e6d575c77724456c0