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Cross-talk between histone H3 tails produces cooperative nucleosome acetylation

热1 corelboy 添加于 2009-11-26 23:35 | 1840 次阅读 | 0 个评论

作者
Li S, Shogren-Knaak MA
摘要
Acetylation of histone proteins by the yeast Spt-Ada-Gcn5-acetyltansferase (SAGA) complex has served as a paradigm for understanding how posttranslational modifications of chromatin regulate eukaryotic gene expression. Nonetheless, it has been unclear to what extent the structural complexity of the chromatin substrate modulates SAGA activity. By using chromatin model systems, we have found that SAGA-mediated histone acetylation is highly cooperative (cooperativity constant of 1.97 +/- 0.15), employing the binding of multiple noncontiguous nucleosomes to facilitate maximal acetylation activity. Studies with various chromatin substrates, including those containing novel asymmetric histone octamers, indicate that this cooperativity occurs only when both H3 histone tails within a nucleosome are properly oriented and unacetylated. We propose that modulation of maximal SAGA activity through this dual-tail recognition could facilitate coregulation of spatially proximal genes by promoting cooperative nucleosome acetylation between genes.
详细资料
- 关键词: Acetylation; Chromatin/metabolism; Histones/*metabolism; Kinetics; Nucleosomes/*metabolism; Protein Binding; Saccharomyces cerevisiae/enzymology; Saccharomyces cerevisiae Proteins/metabolism; Trans-Activators/metabolism
- 文献种类:期刊
- 期刊名称: Proceedings of the National Academy of Sciences of the United States of America
- 期刊缩写: Proc Natl Acad Sci U S A
- 期卷页: 2008年第105卷第47期 18243-18248页
- 地址: Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, IA 50011, USA
- ISBN: 1091-6490
- 备注:PMID:19004784
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