Characterization of lysine 56 of histone H3 as an acetylation site in Saccharomyces cerevisiae
Characterization of lysine 56 of histone H3 as an acetylation site in Saccharomyces cerevisiae
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DOI：
10.1074/jbc.c500181200
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发表时间：
2005-07-15
影响因子：
4.8
通讯作者：
Logie, C
中科院分区：
文献类型：
--
作者：
Ozdemir, A;Spicuglia, S;Logie, C
翻译后组蛋白修饰比比皆是，并调节多个核过程。大多数修饰针对组蛋白的氨基末端结构域。在这里，我们报告了组蛋白H3核心结构域内赖氨酸56乙酰化的鉴定和表征。在核小体的晶体结构中，赖氨酸56触点DNA。表型分析表明，赖氨酸56对组蛋白功能至关重要，并且它调节甲酰胺耐药性，紫外线辐射敏感性和对羟基脲的敏感性。我们表明，在相间，中期和S相期间，组蛋白H3赖氨酸56（H3-K56）的乙酰化形式存在。最后，反向遗传分析表明，酿酒酵母中，均不导致已知的组蛋白乙酰转移酶完全负责H3-K56乙酰化。
Post-translational histone modifications abound and regulate multiple nuclear processes. Most modifications are targeted to the amino-terminal domains of histones. Here we report the identification and characterization of acetylation of lysine 56 within the core domain of histone H3. In the crystal structure of the nucleosome, lysine 56 contacts DNA. Phenotypic analysis suggests that lysine 56 is critical for histone function and that it modulates formamide resistance, ultraviolet radiation sensitivity, and sensitivity to hydroxyurea. We show that the acetylated form of histone H3 lysine 56 (H3-K56) is present during interphase, metaphase, and S phase. Finally, reverse genetic analysis indicates that none of the known histone acetyltransferases is solely responsible for H3-K56 acetylation in Saccharomyces cerevisiae.