Structural basis for recognition of H3K56-acetylated histone H3–H4 by the chaperone Rtt106
Dan Su,
Qi Hu,
Qing Li,
James R. Thompson,
Gaofeng Cui,
Ahmed Fazly,
Brian A. Davies,
Maria Victoria Botuyan,
Zhiguo Zhang () and
Georges Mer ()
Additional contact information
Dan Su: Mayo Clinic
Qi Hu: Mayo Clinic
Qing Li: Mayo Clinic
James R. Thompson: Mayo Clinic
Gaofeng Cui: Mayo Clinic
Ahmed Fazly: Mayo Clinic
Brian A. Davies: Mayo Clinic
Maria Victoria Botuyan: Mayo Clinic
Zhiguo Zhang: Mayo Clinic
Georges Mer: Mayo Clinic
Nature, 2012, vol. 483, issue 7387, 104-107
Abstract:
Direct binding of Rtt106 to H3K56-acetylated (H3–H4)2 histone tetramers contributes to nucleosome assembly with implications for DNA replication, gene silencing and maintenance of genomic stability.
Date: 2012
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Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:483:y:2012:i:7387:d:10.1038_nature10861
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DOI: 10.1038/nature10861
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