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Journal Article

Structure and VP16 binding of the Mediator Med25 activator interaction domain

MPS-Authors
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Cramer,  P.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Fulltext (public)

1937769.pdf
(Publisher version), 2MB

Supplementary Material (public)

1937769-Suppl.pdf
(Supplementary material), 530KB

Citation

Vojnic, E., Mourão, A., Seizl, M., Simon, B., Wenzeck, L., Larivière, L., et al. (2011). Structure and VP16 binding of the Mediator Med25 activator interaction domain. Nature Structural and Molecular Biology, 18(4), 404-409. doi:10.1038/nsmb.1997.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0015-81BF-6
Abstract
Eukaryotic transcription is regulated by interactions between gene-specific activators and the coactivator complex Mediator. Here we report the NMR structure of the Mediator subunit Med25 (also called Arc92) activator interaction domain (ACID) and analyze the structural and functional interaction of ACID with the archetypical acidic transcription activator VP16. Unlike other known activator targets, ACID forms a seven-stranded β-barrel framed by three helices. The VP16 subdomains H1 and H2 bind to opposite faces of ACID and cooperate during promoter-dependent activated transcription in a in vitro system. The activator-binding ACID faces are functionally required and conserved among higher eukaryotes. Comparison with published activator structures reveals that the VP16 activation domain uses distinct interaction modes to adapt to unrelated target surfaces and folds that evolved for activator binding.