Lysine crotonylation is a posttranslational modification (PTM) of histone proteins originally identified by Tan et al.1. This novel evolutionarily conserved histone modification was identified on 28 lysine sites on various histones1. Lysine crotonylation occurs primarily on the ε-amino group of lysine, but its planar orientation and four-carbon length distinguish it from lysine acetylation. Histone crotonylation specifically labels the enhancers and transcription starting sites of active genes in both the human somatic cell genome and the murine male germ cell genome. Histone crotonylation, like acetylation, affects chromatin structure and facilitates histone replacement in elongating spermatids1. Recently YEATS domain-containing protein YEATS2 was found to be a selective histone crotonylation reader2.

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非组蛋白蛋白质上巴豆酰化的全球概况

赖氨酸巴豆酰化是Tan等人最初发现的组蛋白的翻译后修饰（PTM）。在各种组蛋白的28个赖氨酸位点上发现了这种新颖的进化保守组蛋白修饰。赖氨酸巴豆酰化主要发生在赖氨酸的ε-氨基上，但其平面取向和四碳长度使其与赖氨酸乙酰化区分开。组蛋白巴豆酰化特别标记了人类体细胞基因组和鼠雄性生殖细胞基因组中活性基因的增强子和转录起始位点。组蛋白巴豆酰化与乙酰化一样，会影响染色质的结构并促进组蛋白在延长精子中的替换1。最近，发现含有YEATS结构域的蛋白质YEATS2是选择性的组蛋白巴豆酰化阅读器2。