组蛋白 SUMO 化与染色质动力学。
Histone sumoylation and chromatin dynamics.
机构信息
School of Life Sciences, BK21 FOUR KNU Creative BioResearch Group, College of National Sciences, Kyungpook National University, Daegu 41566, Republic of Korea.
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
出版信息
Nucleic Acids Res. 2021 Jun 21;49(11):6043-6052. doi: 10.1093/nar/gkab280.
Chromatin structure and gene expression are dynamically controlled by post-translational modifications (PTMs) on histone proteins, including ubiquitylation, methylation, acetylation and small ubiquitin-like modifier (SUMO) conjugation. It was initially thought that histone sumoylation exclusively suppressed gene transcription, but recent advances in proteomics and genomics have uncovered its diverse functions in cotranscriptional processes, including chromatin remodeling, transcript elongation, and blocking cryptic initiation. Histone sumoylation is integral to complex signaling codes that prime additional histone PTMs as well as modifications of the RNA polymerase II carboxy-terminal domain (RNAPII-CTD) during transcription. In addition, sumoylation of histone variants is critical for the DNA double-strand break (DSB) response and for chromosome segregation during mitosis. This review describes recent findings on histone sumoylation and its coordination with other histone and RNAPII-CTD modifications in the regulation of chromatin dynamics.
染色质结构和基因表达受组蛋白翻译后修饰（PTMs）的动态调控，包括泛素化、甲基化、乙酰化和小泛素样修饰（SUMO）缀合。最初认为组蛋白 SUMO 化仅抑制基因转录，但蛋白质组学和基因组学的最新进展揭示了其在共转录过程中的多种功能，包括染色质重塑、转录延伸和阻断隐匿起始。组蛋白 SUMO 化是复杂信号代码的组成部分，该代码可在转录过程中预先修饰其他组蛋白以及 RNA 聚合酶 II 羧基末端结构域（RNAPII-CTD）。此外，组蛋白变体的 SUMO 化对于 DNA 双链断裂（DSB）反应和有丝分裂期间的染色体分离至关重要。这篇综述描述了组蛋白 SUMO 化及其与其他组蛋白和 RNAPII-CTD 修饰在调控染色质动力学中的协调作用的最新发现。
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