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Article

Mutational analysis of the Sir3 BAH domain reveals multiple points of interaction with nucleosomes.

Molecular and cellular biology - 1 May 2009

Sampath Vinaya, Yuan Peihua, Wang Isabel X, Prugar Evelyn, van Leeuwen Fred, Sternglanz Rolf

Abstract excerpt

Sir3, a component of the transcriptional silencing complex in the yeast Saccharomyces cerevisiae, has an N-terminal BAH domain that is crucial for the protein's silencing function. Previous work has shown that the N-terminal alanine residue of Sir3 (Ala2) and its acetylation play an important role in silencing. Here we show that the silencing defects of Sir3 Ala2 mutants can be suppressed by mutations in histones...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 19273586
DOI: 10.1128/MCB.01682-08
PMCID: PMC2682052

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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