Gill Grace
Department of Pathology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115, USA.
Curr Opin Genet Dev. 2005 Oct;15(5):536-41. doi: 10.1016/j.gde.2005.07.004.
Many proteins that are important for regulated gene expression--including promoter-specific transcription factors, cofactors and chromatin-modifying enzymes--have been found to be reversibly modified by the small ubiquitin-related modifier, SUMO. Post-translational modification by SUMO has diverse effects on substrate activity, but, in most cases described to date, SUMOylation of transcriptional regulators correlates with inhibition of transcription. Recent studies provide new insights into the mechanisms by which SUMOylation regulates transcription and suggest that one consequence of SUMOylation is to promote the interaction of transcription factors with co-repressors. Histone deacetylase co-repressors have been found to function as substrates, effectors, and regulators of SUMOylation, suggesting that complex crosstalk between acetylation and SUMOylation is important for gene regulation.
许多对基因表达调控至关重要的蛋白质，包括启动子特异性转录因子、辅因子和染色质修饰酶，已被发现可被小泛素相关修饰物SUMO进行可逆修饰。SUMO的翻译后修饰对底物活性有多种影响，但在迄今为止描述的大多数情况下，转录调节因子的SUMO化与转录抑制相关。最近的研究为SUMO化调节转录的机制提供了新的见解，并表明SUMO化的一个结果是促进转录因子与共抑制因子的相互作用。组蛋白去乙酰化酶共抑制因子已被发现作为SUMO化的底物、效应器和调节因子发挥作用，这表明乙酰化和SUMO化之间的复杂相互作用对基因调控很重要。
