| First Author | Wissmüller S | Year | 2006 |
| Journal | Nucleic Acids Res | Volume | 34 |
| Issue | 6 | Pages | 1735-44 |
| PubMed ID | 16582099 | Mgi Jnum | J:175179 |
| Mgi Id | MGI:5284787 | Doi | 10.1093/nar/gkl105 |
| Citation | Wissmuller S, et al. (2006) The high-mobility-group domain of Sox proteins interacts with DNA-binding domains of many transcription factors. Nucleic Acids Res 34(6):1735-44 |
| abstractText | 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. |
