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Titolo:
Crystal structure of Negative Cofactor 2 recognizing the TBP-DNA transcription complex
Autore:
Kamada, K; Shu, F; Chen, H; Malik, S; Stelzer, G; Roeder, RG; Meisterernst, M; Burley, SK;
Indirizzi:
Rockefeller Univ, Lab Mol Biophys, New York, NY 10021 USA Rockefeller Univ New York NY USA 10021 ol Biophys, New York, NY 10021 USA Rockefeller Univ, Biochem & Mol Biol Lab, New York, NY 10021 USA Rockefeller Univ New York NY USA 10021 l Biol Lab, New York, NY 10021 USA Rockefeller Univ, Howard Hughes Med Inst, New York, NY 10021 USA Rockefeller Univ New York NY USA 10021 s Med Inst, New York, NY 10021 USA Natl Res Ctr Environm & Hlth, Inst Immunol, Dept Gene Express, D-81377 Munich, Germany Natl Res Ctr Environm & Hlth Munich Germany D-81377 1377 Munich, Germany Univ Munich, Mol Biol Lab, D-81377 Munich, Germany Univ Munich Munich Germany D-81377 Mol Biol Lab, D-81377 Munich, Germany
Titolo Testata:
CELL
fascicolo: 1, volume: 106, anno: 2001,
pagine: 71 - 81
SICI:
0092-8674(20010713)106:1<71:CSONC2>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
RNA-POLYMERASE-II; TATA-BINDING PROTEIN; YEAST TFIIA/TBP/DNA COMPLEX; HISTONE FOLD; IN-VIVO; PREINITIATION COMPLEX; GENE-TRANSCRIPTION; REPRESSOR COMPLEX; MINOR-GROOVE; BOX;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
55
Recensione:
Indirizzi per estratti:
Indirizzo: Burley, SK Rockefeller Univ, Lab Mol Biophys, 1230 York Ave, New York, NY 10021 USA Rockefeller Univ 1230 York Ave New York NY USA 10021 10021 USA
Citazione:
K. Kamada et al., "Crystal structure of Negative Cofactor 2 recognizing the TBP-DNA transcription complex", CELL, 106(1), 2001, pp. 71-81

Abstract

The X-ray structure of a ternary complex of Negative Cofactor 2 (NC2), theTATA box binding protein (TBP), and DNA has been determined at 2.6 Angstrom resolution. The N termini of NC2 alpha and beta resemble histones H2A andH2B, respectively, and form a heterodimer that binds to the bent DNA double helix on the underside of the preformed TBP-DNA complex via electrostaticinteractions. NC2 beta contributes to inhibition of TATA-dependent transcription through interactions of its C-terminal or helix with a conserved hydrophobic feature on the upper surface of TBP, which in turn positions the penultimate a helix of NC2 beta to block recognition of the TBP-DNA complex by transcription factor IIB. Further regulatory implications of the NC2 heterodimer structure are discussed.

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Documento generato il 20/09/20 alle ore 18:36:16