A histone acetylation switch regulates H2A.Z deposition by the SWR-C remodeling enzyme
UMass Chan Affiliations
Program in Molecular MedicineDepartment of Biochemistry and Molecular Pharmacology
Document Type
Journal ArticlePublication Date
2013-04-12Keywords
AcetylationAdenosine Triphosphatases
Biocatalysis
*Chromatin Assembly and Disassembly
Histones
Multienzyme Complexes
Nucleosomes
Protein Multimerization
Protein Stability
Protein Subunits
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Substrate Specificity
Biochemistry
Molecular Biology
Metadata
Show full item recordAbstract
The histone variant H2A.Z plays key roles in gene expression, DNA repair, and centromere function. H2A.Z deposition is controlled by SWR-C chromatin remodeling enzymes that catalyze the nucleosomal exchange of canonical H2A with H2A.Z. Here we report that acetylation of histone H3 on lysine 56 (H3-K56Ac) alters the substrate specificity of SWR-C, leading to promiscuous dimer exchange in which either H2A.Z or H2A can be exchanged from nucleosomes. This result was confirmed in vivo, where genome-wide analysis demonstrated widespread decreases in H2A.Z levels in yeast mutants with hyperacetylated H3K56. Our work also suggests that a conserved SWR-C subunit may function as a "lock" that prevents removal of H2A.Z from nucleosomes. Our study identifies a histone modification that regulates a chromatin remodeling reaction and provides insights into how histone variants and nucleosome turnover can be controlled by chromatin regulators.Source
Science. 2013 Apr 12;340(6129):195-9. doi: 10.1126/science.1229758. Link to article on publisher's siteDOI
10.1126/science.1229758Permanent Link to this Item
http://hdl.handle.net/20.500.14038/30692PubMed ID
23580526Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1126/science.1229758