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Vojnic, E.* ; Mourao, A. ; Seizl, M.* ; Simon, B.* ; Wenzeck, L.* ; Larivière, L.* ; Baumli, S.* ; Baumgart, K.* ; Meisterernst, M.* ; Sattler, M. ; Cramer, P.*

Structure and VP16 binding of the Mediator Med25 activator interaction domain.

Nat. Struct. Mol. Biol. 18, 404-410 (2011)
Verlagsversion DOI PMC
Open Access Gold
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.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Herpes-simplex-virus; RNA-polymerase-II; Transcriptional activation; Transactivation domain; Regulatory protein; Mammalian-cells; DNA-binding; Basal transcription; Cross-Linking; Amino-acids
Sprache englisch
Veröffentlichungsjahr 2011
HGF-Berichtsjahr 2011
ISSN (print) / ISBN 1545-9993
e-ISSN 1545-9985
Zeitschrift Nature Structural & Molecular Biology
Quellenangaben Band: 18, Heft: 4, Seiten: 404-410 Artikelnummer: , Supplement: ,
Verlag Nature Publishing Group
Verlagsort New York, NY
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Structural Biology (STB)
POF Topic(s) 30203 - Molecular Targets and Therapies
Forschungsfeld(er) Enabling and Novel Technologies
PSP-Element(e) G-503000-001
PubMed ID 21378965
DOI 10.1038/nsmb.1997
Scopus ID 79953770655
Erfassungsdatum 2011-09-20
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