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Article

Yeast G1 DNA damage checkpoint regulation by H2A phosphorylation is independent of chromatin remodeling.

Proceedings of the National Academy of Sciences of the United States of America - 12 Sept 2006

Javaheri Ali, Wysocki Robert, Jobin-Robitaille Olivier, Altaf Mohammed, Côté Jacques, Kron Stephen J

Abstract excerpt

Recent studies of yeast G1 DNA damage response have identified characteristic changes in chromatin adjacent to double-strand breaks (DSBs). Histone H2A (yeast H2AX) is rapidly phosphorylated on S129 by the kinase Tel1 (ATM) over a domain extending kilobases from the DSB. The adaptor protein Rad9 (53BP1) is recruited to this chromatin domain through binding of its tudor domains to histone H3 diMe-K79. Multisite...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 16940359
DOI: 10.1073/pnas.0511192103
PMCID: PMC1564209

Genes

INO80
ATM
ATR

Provenance

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Related research

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Research trail→

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Yeast G1 DNA damage checkpoint regulation by H2A phosphorylation is independent of chromatin remodeling.PMID 16940359Read ↗

The functions of budding yeast Sae2 in the DNA damage response require Mec1- and Tel1-dependent phosphorylation.Semantic proximity Read ↗

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Histone H2A phosphorylation controls Crb2 recruitment at DNA breaks, maintains checkpoint arrest, and influences DNA repair in fission yeast.Semantic proximity Read ↗

γH2A is a component of yeast heterochromatin required for telomere elongation.Semantic proximity Read ↗

Rad9 phosphorylation sites couple Rad53 to the Saccharomyces cerevisiae DNA damage checkpoint.Semantic proximity Read ↗

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Tel2 mediates activation and localization of ATM/Tel1 kinase to a double-strand break.Semantic proximity Read ↗

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