Organismal differences in post-translational modifications in histones H3 and H4
Organismal differences in post-translational modifications in histones H3 and H4
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DOI：
10.1074/jbc.m607900200
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发表时间：
2007-03-09
影响因子：
4.8
通讯作者：
Hunt, Donald F.
中科院分区：
文献类型：
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作者：
Garcia, Benjamin A.;Hake, Sandra B.;Hunt, Donald F.
历史的翻译后修饰（PTM）在许多细胞过程中起着重要作用，尤其是基因调节。使用质谱和免疫化学方法的组合，我们表明组蛋白H3的PTM谱在所检查的各种模型生物之间显着不同。例如，与哺乳动物细胞（小鼠和人类）相比，单细胞真核生物，例如酿酒酵母（酵母）（酵母）和四膜hymena hythyphila（TET），其激活比沉默痕迹（小鼠和人类）相比，通常在PTM中富含PTMS中通常与基因沉默更多相关。仔细检查表明，许多众所周知的修饰赖氨酸（LYS）可以是甲基化的或乙酰化的，并且从单细胞真核生物到哺乳动物的总体修饰模式变得更加复杂。此外，还通过质谱法检测了来自野生型细胞的新型物种特异性的H3 PTM。我们的结果表明，某些PTM比以前认为的更保守，包括酵母中的H3K9ME1和H4K20ME2，H3K27ME1，-Me2和-me3在TET中。在组蛋白H4上，Lys-20处的甲基化显示出与Lys-9时H3甲基化相似的模式，哺乳动物含有比单细胞生物更多的甲基化。另外，在所检查的生物体中，H4乙酰化的修饰谱非常相似。
Post-translational modifications (PTMs) of histories play an important role in many cellular processes, notably gene regulation. Using a combination of mass spectrometric and immunobiochemical approaches, we show that the PTM profile of histone H3 differs significantly among the various model organisms examined. Unicellular eukaryotes, such as Saccharomyces cerevisiae (yeast) and Tetrahymena thermophila (Tet), for example, contain more activation than silencing marks as compared with mammalian cells (mouse and human), which are generally enriched in PTMs more often associated with gene silencing. Close examination reveals that many of the better-known modified lysines (Lys) can be either methylated or acetylated and that the overall modification patterns become more complex from unicellular eukaryotes to mammals. Additionally, novel species-specific H3 PTMs from wild-type asynchronously grown cells are also detected by mass spectrometry. Our results suggest that some PTMs are more conserved than previously thought, including H3K9me1 and H4K20me2 in yeast and H3K27me1, -me2, and -me3 in Tet. On histone H4, methylation at Lys-20 showed a similar pattern as H3 methylation at Lys-9, with mammals containing more methylation than the unicellular organisms. Additionally, modification profiles of H4 acetylation were very similar among the organisms examined.