首页> 外文会议>American Society for Mass Spectrometry Conference on Mass Spectrometry and Allied Topics >Substrate Selectivity and Mechanism of the picNuA4 Histone Acetyltransferase Enzyme Complex as Revealed by Isotopic Labeling and LC-MS/MS
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Substrate Selectivity and Mechanism of the picNuA4 Histone Acetyltransferase Enzyme Complex as Revealed by Isotopic Labeling and LC-MS/MS

机译:PICNUA4组氨酸乙酰转移酶酶复合物的基板选择性和机制如同位素标记和LC-MS / MS所示

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(1) Histone modifications are responsible for regulation of diverse cellular processes such as gene transcription. (2) picNuA4 contains Esa1, an essential yeast acetyltransferase responsible for histone H4 acetylation. (3) Here we show: (a) Nucleosome structure restricts picNuA4 histone acetylation; (b) picNuA4 utilizes a dissociative mechanism for H4 acetylation; (c) picNuA4 acetylation order of H4 is random with slight preference for N-terminal lysine residues; (d) Multiple lysine residues of H4 are dispensible for efficient acetylation by picNuA.
机译:(1)组蛋白修饰负责调节不同细胞过程,例如基因转录。 (2)PICNUA4含有ESA1,一种原始酵母乙酰转移酶,负责组蛋白H4乙酰化。 (3)我们展示:(a)核心结构限制PICNUA4组蛋白乙酰化; (b)PICNUA4利用分离机制进行H4乙酰化; (c)H4的PICNUA4乙酰化顺序随机偏好于N-末端赖氨酸残基; (d)H4的多个赖氨酸残基可分配用于通过PICNUA有效乙酰化。

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