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Titolo:
Mutations in both the structured domain and N-terminus of histone H2B bypass the requirement for Swi-Snf in yeast
Autore:
Recht, J; Osley, MA;
Indirizzi:
Mem Sloan Kettering Canc Ctr, Program Mol Biol, New York, NY 10021 USA MemSloan Kettering Canc Ctr New York NY USA 10021 New York, NY 10021 USA Cornell Univ, Grad Sch Med Sci, New York, NY 10021 USA Cornell Univ New York NY USA 10021 ad Sch Med Sci, New York, NY 10021 USA
Titolo Testata:
EMBO JOURNAL
fascicolo: 1, volume: 18, anno: 1999,
pagine: 229 - 240
SICI:
0261-4189(19990104)18:1<229:MIBTSD>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
SACCHAROMYCES-CEREVISIAE; CHROMATIN STRUCTURE; SWI/SNF COMPLEX; NUCLEOSOMAL DNA; IN-VIVO; TRANSCRIPTIONAL ACTIVATORS; GENE ACTIVATION; BINDING PROTEIN; TAIL DOMAINS; ACETYLATION;
Keywords:
chromatin remodeling; histone H2B; transcription; yeast Swi-Snf complex;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
81
Recensione:
Indirizzi per estratti:
Indirizzo: Osley, MA Mem Sloan Kettering Canc Ctr, Program Mol Biol, New York, NY 10021 USA Mem Sloan Kettering Canc Ctr New York NY USA 10021 NY 10021 USA
Citazione:
J. Recht e M.A. Osley, "Mutations in both the structured domain and N-terminus of histone H2B bypass the requirement for Swi-Snf in yeast", EMBO J, 18(1), 1999, pp. 229-240

Abstract

The chromatin elements targeted by the ATP-dependent, Swi-Snf nucleosome-remodeling complex are unknown, To address this question, we generated mutations in yeast histone H2B that suppress phenotypes associated with the absence of Swi-Snf, Sin(Swi-Snf-independent) mutations occur in residues involved in H2A-H2B dimer formation, dimer-tetramer association, and in the H2B N-terminus. The strongest and most pleiotropic Sin(-) mutation removed 20 amino acid residues from the H2B N-terminus, This mutation allowed active chromatin to be formed at the SUC2 locus in a snf5 Delta mutant and resulted in hyperactivated levels of SUC2 mRNA under inducing conditions. Thus, the H2B N-terminus may be an important target of Swi-Snf in vivo. The GCN5 gene product, the catalytic subunit of several nuclear histone acetytransferase complexes that modify histone N-termini, was also found to act in conjunction with Swi-Snf, The phenotypes of double gcn5 Delta snf5 Delta mutants suggest that histone acetylation may play both positive and negative roles in the activity of the Swi-Snf-remodeling factor.

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Documento generato il 20/01/21 alle ore 01:30:17