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Article

Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56.

Science (New York, N.Y.) - 2 Feb 2007

Driscoll Robert, Hudson Amanda, Jackson Stephen P

Abstract excerpt

Posttranslational modifications of the histone octamer play important roles in regulating responses to DNA damage. Here, we reveal that Saccharomyces cerevisiae Rtt109p promotes genome stability and resistance to DNA-damaging agents, and that it does this by functionally cooperating with the histone chaperone Asf1p to maintain normal chromatin structure. Furthermore, we show that, as for Asf1p, Rtt109p is...

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Share to Acetylation
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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 17272722
DOI: 10.1126/science.1135862
PMCID: PMC3334813

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56.PMID 17272722Read ↗

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The Rtt106 histone chaperone is functionally linked to transcription elongation and is involved in the regulation of spurious transcription from cryptic promoters in yeast.Semantic proximity Read ↗

Structural analysis of Rtt106p reveals a DNA binding role required for heterochromatin silencing.Semantic proximity Read ↗

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