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Titolo:
YEAST HISTONE H3 AND H4 AMINO TERMINI ARE IMPORTANT FOR NUCLEOSOME ASSEMBLY IN-VIVO AND IN-VITRO - REDUNDANT AND POSITION-INDEPENDENT FUNCTIONS IN ASSEMBLY BUT NOT IN GENE-REGULATION
Autore:
LING XF; HARKNESS TAA; SCHULTZ MC; FISHERADAMS G; GRUNSTEIN M;
Indirizzi:
UNIV CALIF LOS ANGELES,SCH MED,DEPT BIOL CHEM LOS ANGELES CA 90095 UNIV CALIF LOS ANGELES,SCH MED,DEPT BIOL CHEM LOS ANGELES CA 90095 UNIV CALIF LOS ANGELES,INST MOLEC BIOL LOS ANGELES CA 90095 UNIV ALBERTA,DEPT BIOCHEM EDMONTON AB CANADA
Titolo Testata:
Genes & development
fascicolo: 6, volume: 10, anno: 1996,
pagine: 686 - 699
SICI:
0890-9369(1996)10:6<686:YHHAHA>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
SILENT MATING LOCI; DNA-REPLICATION INVITRO; XENOPUS-LAEVIS OOCYTES; SACCHAROMYCES-CEREVISIAE; CELL-CYCLE; SEQUENCE-ANALYSIS; N-TERMINUS; CHROMATIN; PROTEIN; REPRESSION;
Keywords:
SACCHAROMYCES CEREVISIAE; HISTONE H3; HISTONE H4; NUCLEOSOME ASSEMBLY; GENE EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
54
Recensione:
Indirizzi per estratti:
Citazione:
X.F. Ling et al., "YEAST HISTONE H3 AND H4 AMINO TERMINI ARE IMPORTANT FOR NUCLEOSOME ASSEMBLY IN-VIVO AND IN-VITRO - REDUNDANT AND POSITION-INDEPENDENT FUNCTIONS IN ASSEMBLY BUT NOT IN GENE-REGULATION", Genes & development, 10(6), 1996, pp. 686-699

Abstract

The hydrophilic amino-terminal sequences of histones H3 and H4 extendfrom the highly structured nucleosome core. Here we examine the importance of the amino termini and their position in the nucleosome with regard to both nucleosome assembly and gene regulation. Despite previous conclusions based on nonphysiological nucleosome reconstitution experiments, we find that the histone amino termini are important for nucleosome assembly in vivo and in vitro. Deletion of both tails, a lethalevent, alters micrococcal nuclease-generated nucleosomal ladders, plasmid superhelicity in whole cells, and nucleosome assembly in cell extracts. The H3 and H4 amino-terminal tails have redundant functions in this regard because the presence of either tail allows assembly and cellular viability. Moreover, the tails need not be attached to their native carboxy-terminal core. Their exchange re-establishes both cellular viability and nucleosome assembly. In contrast, the regulation of GAL1 and the silent mating loci by the H3 and H4 tails is highly disrupted by exchange of the histone amino termini.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 07:07:18