Daniel Jeremy A, Grant Patrick A
Department of Biochemistry and Molecular Genetics, University of Virginia School of Medicine, Charlottesville, VA 22908, USA.
Mutat Res. 2007 May 1;618(1-2):135-48. doi: 10.1016/j.mrfmmm.2006.09.008. Epub 2007 Jan 21.
Over the past 10 years, much progress has been made to understand the roles of the similar, yet distinct yeast SAGA and SLIK coactivator complexes involved in histone post-translational modification and gene regulation. Many different groups have elucidated functions of the SAGA complexes including identification of novel components, which have conferred additional distinct functions. Together, recent studies demonstrate unique attributes of the SAGA coactivator complexes in histone acetylation, methylation, phosphorylation, and deubiquitination. In addition to roles in transcriptional activation with the 19S proteasome regulatory particle, recent evidence also suggests functions for SAGA in elongation and mRNA export. The modular nature of SAGA allows this approximately 1.8 MDa complex to organize its functions and carry out multiple roles during transcription, particularly under conditions of cellular stress.
在过去十年中,我们在理解酵母中相似但又不同的SAGA和SLIK共激活因子复合物在组蛋白翻译后修饰和基因调控中的作用方面取得了很大进展。许多不同的研究小组已经阐明了SAGA复合物的功能,包括鉴定出具有额外独特功能的新组分。最近的研究共同证明了SAGA共激活因子复合物在组蛋白乙酰化、甲基化、磷酸化和去泛素化方面的独特特性。除了与19S蛋白酶体调节颗粒一起在转录激活中发挥作用外,最近的证据还表明SAGA在延伸和mRNA输出中也有功能。SAGA的模块化性质使这个大约1.8 MDa的复合物能够组织其功能,并在转录过程中发挥多种作用,特别是在细胞应激条件下。