2 research outputs found
Crystal Structure of Apo MEF2B Reveals New Insights in DNA Binding and Cofactor Interaction
The
myocyte enhancer factor 2 (MEF2) family of transcription factors
plays important roles in developmental processes and adaptive responses.
Although MEF2 proteins are known to bind DNA in the nucleus to regulate
specific gene expression, there are reports that show that MEF2 also
functions in the cytoplasm. Previous structural studies of MEF2 focused
exclusively on DNA-bound MEF2 with and without various corepressors
or coactivators. While these studies have established a comprehensive
structural model of DNA recognition and cofactor recruitment by MEF2,
the structure of MEF2 not bound to DNA, which include cytoplasmic
MEF2 and free MEF2 in the nucleus, is unknown. Here we determined
the structure of the MADS-box/MEF2 domain of MEF2B without DNA nor
cofactor. The Apo structure of MEF2B reveals a largely preformed DNA
binding interface that may be important for recognizing the shape
of DNA from the minor groove side. In addition, our structure also
reveals that the C-terminal helix of the MEF2-specific domain could
flip up to bind to the hydrophobic groove that serves as the binding
sites of MEF2 transcription cofactors. These observations shed new
insights into DNA binding and cofactor interaction by MEF2 proteins