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Expression data from wild-type and H2B K37A mutant yeast histones

ABSTRACT: We identified lysine 37 of histone H2B as a novel site of histone lysine methylation in budding yeast. Microarray analysis was performed to determine global changes in gene expression upon mutation of this lysine residue to a unmodifiable form.

ORGANISM(S): Schizosaccharomyces pombe Saccharomyces cerevisiae

PROVIDER: GSE24380 | GEO | 2010/09/27

SECONDARY ACCESSION(S): PRJNA132865

REPOSITORIES: GEO

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Expression data from wild-type and H2B K37A mutant yeast histones

Project description:We identified lysine 37 of histone H2B as a novel site of histone lysine methylation in budding yeast. Microarray analysis was performed to determine global changes in gene expression upon mutation of this lysine residue to a unmodifiable form. Histones were acid-extracted from asynchronously grown yeast expressing wild-type H2B or H2B harboring a K37A mutation.

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methylation sites of Histone H2B catalyzed by LaeA

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Project description:Nucleosome assembly in vivo requires assembly factors, such as histone chaperones, to bind to histones and mediate their deposition onto DNA. In yeast, the essential histone chaperone FACT (FAcilitates Chromatin Transcription) functions in nucleosome assembly and H2A-H2B deposition during transcription elongation and DNA replication. Recent studies have identified candidate histone residues that mediate FACT binding to histones, but it is not known which histone residues are important for FACT to deposit histones onto DNA during nucleosome assembly. In this study, we report that the histone H2B repression (HBR) domain within the H2B N-terminal tail is important for histone deposition by FACT. Deletion of the HBR domain causes significant defects in histone occupancy in the yeast genome, particularly at HBR-repressed genes, and a pronounced increase in H2A-H2B dimers that remain bound to FACT in vivo. Moreover, the HBR domain is required for purified FACT to efficiently assemble recombinant nucleosomes in vitro. We propose that the interaction between the highly basic HBR domain and DNA plays an important role in stabilizing the nascent nucleosome during the process of histone H2A-H2B deposition by FACT. 6 samples, 2 inputs and 4 ChIP samples for histone H2B (2 for wild-type and 2 for an H2B â30-37 mutant)

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