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Article

Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106.

Nature - 5 Feb 2012

Su Dan, Hu Qi, Li Qing, Thompson James R, Cui Gaofeng, Fazly Ahmed, Davies Brian A, Botuyan Maria Victoria, Zhang Zhiguo, Mer Georges

Abstract excerpt

Dynamic variations in the structure of chromatin influence virtually all DNA-related processes in eukaryotes and are controlled in part by post-translational modifications of histones. One such modification, the acetylation of lysine 56 (H3K56ac) in the amino-terminal α-helix (αN) of histone H3, has been implicated in the regulation of nucleosome assembly during DNA replication and repair, and nucleosome...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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PMID: 22307274
DOI: 10.1038/nature10861
PMCID: PMC3439842

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Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106.PMID 22307274Read ↗

Histone chaperone Rtt106 promotes nucleosome formation using (H3-H4)2 tetramers.Semantic proximity Read ↗

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The Histone Chaperone FACT Contributes to DNA Replication-Coupled Nucleosome Assembly.Semantic proximity Read ↗

Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56.Semantic proximity Read ↗

Histone H3K56 acetylation, CAF1, and Rtt106 coordinate nucleosome assembly and stability of advancing replication forks.Semantic proximity Read ↗

A negatively charged residue in place of histone H3K56 supports chromatin assembly factor association but not genotoxic stress resistance.Semantic proximity Read ↗

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