Wegner M (2006)
Publication Type: Journal article, Original article
Publication year: 2006
Publisher: Oxford University Press (OUP): Policy C - Option B / Oxford University Press
Pages Range: 1735-1744
Journal Issue: 34
DOI: 10.1093/nar/gkl105
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. © 2006 Oxford University Press.
APA:
Wegner, M. (2006). The High-mobility-group domain of Sox proteins interacts with the DNA-binding domains of many transcription factors. Nucleic Acids Research, 34, 1735-1744. https://dx.doi.org/10.1093/nar/gkl105
MLA:
Wegner, Michael. "The High-mobility-group domain of Sox proteins interacts with the DNA-binding domains of many transcription factors." Nucleic Acids Research 34 (2006): 1735-1744.
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