Authors: | Recht, J.; Osley, M. A. |
Article Title: | Mutations in both the structured domain and N-terminus of histone H2B bypass the requirement for Swi-Snf in yeast |
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 snf5Δ 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 gcn5Δsnf5Δ mutants suggest that histone acetylation may play both positive and negative roles in the activity of the Swi-Snf-remodeling factor. |
Keywords: | controlled study; mutation; dna-binding proteins; nonhuman; mutant protein; protein conformation; protein domain; phenotype; chromosomal proteins, non-histone; gene targeting; protein kinases; gene locus; transcription factors; amino acid sequence; molecular sequence data; amino terminal sequence; messenger rna; saccharomyces cerevisiae; chromatin; transcription; dimerization; mutagenesis, site-directed; yeast; saccharomyces cerevisiae proteins; histone h2b; histones; protein structure, secondary; acetylation; nucleosomes; fungal proteins; glycoside hydrolases; genes, fungal; histone acetyltransferase; histone acetyltransferases; chromatin remodeling; priority journal; article; yeast swi-snf complex; beta-fructofuranosidase |
Journal Title: | EMBO Journal |
Volume: | 18 |
Issue: | 1 |
ISSN: | 0261-4189 |
Publisher: | Wiley Blackwell |
Date Published: | 1999-01-04 |
Start Page: | 229 |
End Page: | 240 |
Language: | English |
DOI: | 10.1093/emboj/18.1.229 |
PUBMED: | 9878065 |
PROVIDER: | scopus |
PMCID: | PMC1171117 |
DOI/URL: | |
Notes: | Article -- Export Date: 16 August 2016 -- Source: Scopus |