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Titolo:
Histone H2A.Z acetylation modulates an essential charge patch
Autore:
Ren, QH; Gorovsky, MA;
Indirizzi:
Univ Rochester, Dept Biol, Rochester, NY 14627 USA Univ Rochester Rochester NY USA 14627 Dept Biol, Rochester, NY 14627 USA
Titolo Testata:
MOLECULAR CELL
fascicolo: 6, volume: 7, anno: 2001,
pagine: 1329 - 1335
SICI:
1097-2765(200106)7:6<1329:HHAMAE>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
TETRAHYMENA-THERMOPHILA; GENE REPLACEMENT; IN-VIVO; CHROMATIN; VARIANT; PHOSPHORYLATION; NUCLEOSOME; TRANSCRIPTION; DEACETYLASES; YEAST;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
54
Recensione:
Indirizzi per estratti:
Indirizzo: Gorovsky, MA Univ Rochester, Dept Biol, Rochester, NY 14627 USA Univ Rochester Rochester NY USA 14627 ochester, NY 14627 USA
Citazione:
Q.H. Ren e M.A. Gorovsky, "Histone H2A.Z acetylation modulates an essential charge patch", MOL CELL, 7(6), 2001, pp. 1329-1335

Abstract

Histone H2A.Z is structurally and functionally distinct from the major H2As. To understand the function of H2A.Z acetylation, we performed a mutagenic analysis of the six acetylated lysines in the N-terminal tail of Tetrahymena H2A.Z. Tetrahymena cannot survive with arginines at all six sites. Retention of one acetylatable lysine is sufficient to provide the essential function of H2A.Z acetylation. This essential function can be mimicked by deleting the region encompassing all six sites, or by mutations that reduce thepositive charge of the N terminus at the acetylation sites themselves, or at other sites in the tail. These properties argue that the essential function of H2A.Z acetylation is to modify a "charge patch" by reducing the charge of the tail.

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Documento generato il 09/04/20 alle ore 13:28:33