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- Title
Solution structure of the MEF2A-DNA complex: structural basis for the modulation of DNA bending and specificity by MADS-box transcription factors.
- Authors
Kau Huang; Louis, John M.; Donaldson, Logan; Fei-Ling Lim; Sharrocks, Andrew D.; Clore, G. Marius
- Abstract
The solution structure of the 33 kDa complex between the dimeric DNA-binding core domain of the transcription factor MEF2A (residues 1&ndash85) and a 20mer DNA oligonucleotide comprising the consensus sequence CTA(A/T)4TAG has been solved by NMR. The protein comprises two domains: a MADS-box (residues 1&ndash58) and a MEF2S domain (residues 59&ndash 73). Recognition and specificity are achieved by interactions between the MADS-box and both the major and minor grooves of the DNA. A number of critical differences in protein-DNA contacts observed in the MEF2A-DNA complex and the DNA complexes of the related MADS-box transcription factors SRF and MCM1 provide a molecular explanation for modulation of sequence specificity and extent of DNA bending (∼15 versus ∼70°). The structure of the MEF2S domain is entirely different from that of the equivalent SAM domain in SRF and MCM1, accounting for the absence of cross-reactivity with other proteins that interact with these transcription factors.
- Subjects
DNA; DNA-binding proteins; TRANSCRIPTION factors; OLIGONUCLEOTIDES; NUCLEOTIDE sequence; GENETIC transcription
- Publication
EMBO Journal, 2000, Vol 19, Issue 11, p2615
- ISSN
0261-4189
- Publication type
Article
- DOI
10.1093/emboj/19.11.2615