CBP/p300-mediated acetylation of histone H3 on lysine 56
Chandrima Das,
M. Scott Lucia,
Kirk C. Hansen and
Jessica K. Tyler ()
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Chandrima Das: Department of Biochemistry and Molecular Genetics,
M. Scott Lucia: and
Kirk C. Hansen: Cancer Center Proteomics Core, University of Colorado School of Medicine, PO Box 6511, Aurora Colorado 80045, USA
Jessica K. Tyler: Department of Biochemistry and Molecular Genetics,
Nature, 2009, vol. 459, issue 7243, 113-117
Abstract:
Chromatin packaging: H3K56ac makes its mark An acetylation mark within the core domain of histone H3, on lysine 56 (H3K56ac), has an important role in chromatin assembly during DNA replication and repair in budding yeast, but it has not been studied in multicellular eukaryotes. Here, two histone acetyl transferase enzymes are shown to acetylate H3K56 in Drosophila and human cells. Histones carrying K56ac are enriched at sites of DNA repair and elevated in several types of cancer.
Date: 2009
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Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:459:y:2009:i:7243:d:10.1038_nature07861
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DOI: 10.1038/nature07861
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