Sequence and Structure
All of the mammalian Mef2 genes share approximately 50% overall amino acid identity and about 95% similarity throughout the highly conserved N-terminal MADS-box and Mef2 domains, however their sequences diverge in their C-terminal transactivation domain (see figure to the right).
The MADS-box serves as the minimal DNA-binding domain, however an adjacent 29-amino acid extension called the Mef2 domain is required for high affinity DNA-binding and dimerization. Through an interaction with the MADS-box, Mef2 transcription factors have the ability to homo- and heterodimerize, and a classic nuclear localization sequence (NLS) in the C-terminus of Mef2A, -C, and – D ensures nuclear localization of the protein. Interestingly, D-Mef2 and human MEF2B lack this conserved NLS but are still found in the nucleus.
Read more about this topic: Mef2
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“Reminiscences, even extensive ones, do not always amount to an autobiography.... For autobiography has to do with time, with sequence and what makes up the continuous flow of life. Here, I am talking of a space, of moments and discontinuities. For even if months and years appear here, it is in the form they have in the moment of recollection. This strange form—it may be called fleeting or eternal—is in neither case the stuff that life is made of.”
—Walter Benjamin (1892–1940)
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