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  Phosphorylation of histone H3 Ser10 establishes a hierarchy for subsequent intramolecular modification events.

Liokatis, S., Stützer, A., Elsässer, S. J., Theillet, F. X., Klingberg, R., van Rossum, B., et al. (2012). Phosphorylation of histone H3 Ser10 establishes a hierarchy for subsequent intramolecular modification events. Nature Structural and Molecular Biology, 19(8), 819-823. doi:10.1038/nsmb.2310.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000F-EF34-F Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-1DE5-5
Genre: Journal Article

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 Creators:
Liokatis, S., Author
Stützer, A.1, Author              
Elsässer, S. J., Author
Theillet, F. X., Author
Klingberg, R., Author
van Rossum, B., Author
Schwarzer, D., Author
Allis, C. D., Author
Fischle, W.1, Author              
Selenko, P., Author
Affiliations:
1Research Group of Chromatin Biochemistry, MPI for biochemical chemistry, Max Planck Society, ou_578604              

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 Abstract: Phosphorylation of Ser10 of histone H3 regulates chromosome condensation and transcriptional activity. Using time-resolved, high-resolution NMR spectroscopy, we demonstrate that histone H3 Ser10 phosphorylation inhibits checkpoint kinase 1 (Chk1)- and protein kinase C (PKC)-mediated modification of Thr11 and Thr6, the respective primary substrate sites of these kinases. On unmodified H3, both enzymes also target Ser10 and thereby establish autoinhibitory feedback states on individual H3 tails. Whereas phosphorylated Ser10 does not affect acetylation of Lys14 by Gcn5, phosphorylated Thr11 impedes acetylation. Our observations reveal mechanistic hierarchies of H3 phosphorylation and acetylation events and provide a framework for intramolecular modification cross-talk within the N terminus of histone H3.

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Language(s): eng - English
 Dates: 2012-07-152012-08
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/nsmb.2310
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Title: Nature Structural and Molecular Biology
Source Genre: Journal
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Pages: - Volume / Issue: 19 (8) Sequence Number: - Start / End Page: 819 - 823 Identifier: -