Posttranslational modification (PTM) of proteins is used to regulate protein activity and stability. Histone PTMs are regarded as some of the most important, as they can directly regulate gene expression through chromatin reorganization. Recently, histone proteins were found to undergo succinylation, adding to other well-known PTMs such as acetylation, methylation, and phosphorylation. However, there is little information regarding the enzyme which catalyzes histone lysine succinylation. In fact, it is unclear whether this reaction is enzymatic. In this study, we tested histone succinylation activity in vitro using cell nuclear extracts of HepG2 cells. Although whole nuclear extracts did not show histone succinylation activity, we found that an SP 1.0 M KCl fraction of nuclear extracts indeed had such activity. These data offer the first direct evidence that histone succinylation is an enzymatic PTM as are other histone codes in the nucleus.
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机译：蛋白质的翻译后修饰（PTM）用于调节蛋白质活性和稳定性。组蛋白PTM被认为是最重要的，因为它们可以通过染色质重组直接调节基因表达。最近，发现组蛋白经过琥珀酰化作用，并添加到其他众所周知的PTM中，例如乙酰化，甲基化和磷酸化。然而，关于催化组蛋白赖氨酸琥珀酰化的酶的信息很少。实际上，尚不清楚该反应是否是酶促的。在这项研究中，我们使用HepG2细胞的细胞核提取物在体外测试了组蛋白琥珀酰化活性。尽管全核提取物未显示组蛋白琥珀酰化活性，但我们发现核提取物的SP 1.0 M KCl馏分确实具有这种活性。这些数据提供了直接的直接证据，证明组蛋白琥珀酰化是一种酶促的PTM，就像细胞核中的其他组蛋白编码一样。
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