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Titolo:
The histone H4 acetyltransferase MOF uses a C2HC zinc finger for substraterecognition
Autore:
Akhtar, A; Becker, PB;
Indirizzi:
Univ Munich, Adolf Butenandt Inst, Munich, Germany Univ Munich Munich Germany unich, Adolf Butenandt Inst, Munich, Germany
Titolo Testata:
EMBO REPORTS
fascicolo: 2, volume: 2, anno: 2001,
pagine: 113 - 118
SICI:
1469-221X(200102)2:2<113:THHAMU>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
DOSAGE COMPENSATION; X-CHROMOSOME; LIM DOMAIN; DROSOPHILA; PROTEIN; BINDING; TRANSCRIPTION; ASSOCIATION; COMPLEXES; VIRUS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
27
Recensione:
Indirizzi per estratti:
Indirizzo: Becker, PB Univ Munich, Adolf Butenandt Inst, Marchioninistr 15, Munich, Germany Univ Munich Marchioninistr 15 Munich Germany Munich, Germany
Citazione:
A. Akhtar e P.B. Becker, "The histone H4 acetyltransferase MOF uses a C2HC zinc finger for substraterecognition", EMBO REP, 2(2), 2001, pp. 113-118

Abstract

Site-specific acetylation of histone H4 by MOF is central to establishing the hyperactive male X chromosome in Drosophila. MOF belongs to the MYST family of histone acetyltransferases (HATs) characterized by an unusual C2HC-type zinc finger close to their HAT domains. The function of these rare zinc fingers is unknown. We found that this domain is essential for HAT activity, in addition to the established catalytic domain. MOF uses its zinc finger to contact the globular part of the nucleosome as well as the histone H4N-terminal tail substrate. Point mutations that leave the zinc-finger structure intact nevertheless abolish its interaction with the nucleosome. Our data document a novel role of the C2HC-type finger in nucleosome binding and HAT activity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/04/20 alle ore 03:35:02