Histone H3-K56 acetylation is catalyzed by histone chaperone-dependent complexes
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Authors
Tsubota, ToshiakiBerndsen, Christopher E.
Erkmann, Judith A.
Smith, Corey Lewis
Yang, Lanhao
Freitas, Michael A.
Denu, John M.
Kaufman, Paul D.
UMass Chan Affiliations
Program in Gene Function and ExpressionDocument Type
Journal ArticlePublication Date
2007-02-27Keywords
AcetylationAmino Acid Sequence
Amino Acids
Animals
Catalysis
Cell Cycle Proteins
Chickens
Coenzymes
DNA, Fungal
Histone Acetyltransferases
Histones
Kinetics
Lysine
Mass Spectrometry
Molecular Chaperones
Molecular Sequence Data
Multiprotein Complexes
Protein Binding
Protein Subunits
Recombinant Proteins
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Substrate Specificity
Life Sciences
Medicine and Health Sciences
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Show full item recordAbstract
Acetylation of histone H3 on lysine 56 occurs during mitotic and meiotic S phase in fungal species. This acetylation blocks a direct electrostatic interaction between histone H3 and nucleosomal DNA, and the absence of this modification is associated with extreme sensitivity to genotoxic agents. We show here that H3-K56 acetylation is catalyzed when Rtt109, a protein that lacks significant homology to known acetyltransferases, forms an active complex with either of two histone binding proteins, Asf1 or Vps75. Rtt109 binds to both these cofactors, but not to histones alone, forming enzyme complexes with kinetic parameters similar to those of known histone acetyltransferase (HAT) enzymes. Therefore, H3-K56 acetylation is catalyzed by a previously unknown mechanism that requires a complex of two proteins: Rtt109 and a histone chaperone. Additionally, these complexes are functionally distinct, with the Rtt109/Asf1 complex, but not the Rtt109/Vps75 complex, being critical for resistance to genotoxic agents.Source
Mol Cell. 2007 Mar 9;25(5):703-12. Epub 2007 Feb 22. Link to article on publisher's site
DOI
10.1016/j.molcel.2007.02.006Permanent Link to this Item
http://hdl.handle.net/20.500.14038/38460PubMed ID
17320445Related Resources
ae974a485f413a2113503eed53cd6c53
10.1016/j.molcel.2007.02.006
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