Department of Anatomy and Cellular Biology, Tufts University School of Medicine, Boston, MA, USA.
Epigenetics. 2009 Oct 1;4(7):440-4. doi: 10.4161/epi.4.7.9807. Epub 2009 Oct 14.
Post-translational modification of many transcription factors and cofactors by the small ubiquitin-related modifier SUMO has been correlated with transcriptional repression. Recent investigations of the molecular mechanisms underlying SUMO-dependent repression have identified diverse chromatin modifying enzymes and chromatin associated proteins as effectors of SUMO-dependent changes in chromatin structure and gene expression. A surprising diversity of proteins has been identified to be recruited to promoters in a SUMO-dependent manner, including the histone deacetylase HDAC2, the histone demethylase LSD1, the histone methyltransferase SETDB1, the nucleosome remodeling ATPase Mi-2, and chromatin-associated proteins HP1 and L3MBTL1 and L3MBTL2. These findings suggest that SUMOylation plays a central role in coordinating histone modifications and chromatin structure important for regulation of gene expression.
许多转录因子和辅助因子的翻译后修饰被小分子泛素相关修饰物 SUMO 所修饰,这与转录抑制有关。最近对 SUMO 依赖性抑制的分子机制的研究已经确定了多种染色质修饰酶和与染色质相关的蛋白质作为 SUMO 依赖性染色质结构和基因表达变化的效应物。已经鉴定出许多以 SUMO 依赖性方式被招募到启动子的蛋白质,包括组蛋白去乙酰化酶 HDAC2、组蛋白去甲基化酶 LSD1、组蛋白甲基转移酶 SETDB1、核小体重塑 ATP 酶 Mi-2,以及与染色质相关的蛋白质 HP1 和 L3MBTL1 和 L3MBTL2。这些发现表明,SUMO 化在协调组蛋白修饰和染色质结构方面发挥着核心作用,这些修饰和结构对于基因表达的调控至关重要。