Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 18, Issue 4, Pages 404-U29Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1997
Keywords
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Funding
- Boehringer Ingelheim Fonds
- Elitenetzwerk Bayern
- Portuguese Foundation for Science and Technology (FCT) [SFRH/BD/22323/2005]
- Deutsche Forschungsgemeinschaft
- European Commission [LSHG-CT-2005-512028]
- Bavarian NMR Center
- Deutsche Forschungsgemeinschaft [Sonderforschungsbereich SFB646, SFB Transregio 5]
- Jung-Stiftung
- Fonds der chemischen Industrie
- Fundação para a Ciência e a Tecnologia [SFRH/BD/22323/2005] Funding Source: FCT
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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 beta-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.
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