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- Title
The high-mobility-group domain of Sox proteins interacts with DNA-binding domains of many transcription factors.
- Authors
Wissmüller, Sandra; Kosian, Thomas; Wolf, Michael; Finzsch, Markus; Wegner, Michael
- Abstract
Sox proteins are widely believed to team up with other transcription factors as partner proteins to perform their many essential functions during development. In this study, yeast two-hybrid screens identified transcription factors as a major group of interacting proteins for Sox8 and Sox10. Interacting transcription factors were very similar for these two group E Sox proteins and included proteins with different types of DNA-binding domains, such as homeodomain proteins, zinc finger proteins, basic helix-loop-helix and leucine zipper proteins. In all cases analyzed, the interaction involved the DNA-binding domain of the transcription factor which directly contacted the C-terminal part of the high-mobility-group (HMG) domain. In particular, the C-terminal tail region behind helix 3 of the HMG domain was shown by mutagenesis to be essential for interaction and transcription factor recruitment. The HMG domain thus not only possesses DNA-binding and DNA-bending but also protein-interacting ability which may be equally important for the architectural function of Sox proteins on their target gene promoters.
- Publication
Nucleic acids research, 2006, Vol 34, Issue 6, p1735
- ISSN
1362-4962
- Publication type
Journal Article
- DOI
10.1093/nar/gkl105