Functional analysis of histones H2A and H2B in transcriptional repression in Saccharomyces cerevisiae Journal Article


Authors: Recht, J.; Dunn, B.; Raff, A.; Osley, M. A.
Article Title: Functional analysis of histones H2A and H2B in transcriptional repression in Saccharomyces cerevisiae
Abstract: The presence of H2A-H2B dimers in nucleosomes can inhibit the binding of transcription factors to chromatin templates. To study the roles of histones H2A and H2B in transcriptional repression in vivo, mutant forms of these histones were analyzed in two different assay systems. Two repression domains were identified in H2A. One domain includes residues that fall in the beginning of the H2A-H2B dimerization region, and the second is in the H2A N terminus, a region of potential interactions with nonhistone proteins. The function of H2A and H2B in one repression assay was found to be dependent on three SPT (suppressor of Ty) genes whose products are important for chromatin-mediated repression. These results suggest that repressive chromatin structure may be established through the interactions of the Spt proteins with these histones. In contrast, other proteins, the products of the HIR (histone regulation) genes, may function to direct H2A and H2B to specific promoters.
Keywords: promoter region; mutation; nonhuman; protein conformation; chromosomal proteins, non-histone; transcription, genetic; molecular sequence data; saccharomyces cerevisiae; histone; base sequence; binding sites; dna primers; repressor proteins; histones; gene expression regulation, fungal; protein dna interaction; chromatin structure; dna, fungal; nucleosome; transcription termination; fungal proteins; genes, fungal; promoter regions (genetics); suppression, genetic; priority journal; article
Journal Title: Molecular and Cellular Biology
Volume: 16
Issue: 6
ISSN: 0270-7306
Publisher: American Society for Microbiology  
Date Published: 1996-06-01
Start Page: 2545
End Page: 2553
Language: English
PUBMED: 8649361
PROVIDER: scopus
PMCID: PMC231244
DOI: 10.1128/MCB.16.6.2545
DOI/URL:
Notes: Article -- Export Date: 22 November 2017 -- Source: Scopus
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  1. Mary Ann Osley
    17 Osley