染色质乙酰化相关BRD蛋白家族  

Chromatin acetylation associated BRD protein family

作　　者：李军林[1] 张美杰[1] 高晓彩[1] 

机构地区：[1]西北大学生命科学学院,西安710069

出　　处：《生命的化学》2012年第2期169-173,共5页Chemistry of Life

基　　金：国家自然科学基金项目(31071103);西部资源生物与现代生物技术教育部重点实验室开放基金(ZS11005);西北大学自然科学基金(NH10001);西北大学科研启动金(PR10066)资助

摘　　要：Bromodomain结构域首先在果蝇蛋白质Brahma中发现,折叠模式独特且高度保守,是最早也是截至目前公认唯一可与乙酰化赖氨酸结合的结构域。BRD蛋白通过结合不同的蛋白质或者定位蛋白质到细胞核发挥精细调节作用。BRD蛋白复合物常特异性识别并结合到染色质组蛋白H3/H4特定的乙酰化赖氨酸残基,从而影响靶基因的转录翻译;该蛋白复合物功能异常通常与多种疾病的发生相关联,表明对转录翻译调节有重要意义。但迄今为止,BRD蛋白复合物修饰染色质机理不明,现有研究提示BRD蛋白复合物维持染色质乙酰化状态,也可以与染色质组蛋白其它位点结合,从整体水平增强组蛋白乙酰化精度和效率。Bromodomain is identified in Drosophila protein Brahma firstly,characterized with its peculiar and highly conservative folding structure.It is also the first and the only domain that can bind to acetylated lysine by far.The BRD proteins play fine regulation roles through binding other proteins or allocating other proteins into nucleus.The BRD complex influences transcription and expression of target genes through specially binding to acetylated lysine at the loci of H3 and H4 with its ‘hydrophobic pocket’.The abnormal function of BRD complex is associated with various diseases exhibiting an essential role in regulating on genes transcription and translation.However,the modification mechanism by BRD proteins complex is still obscure.Recent research has suggested that chromatin acetylation state is maintained by BRD proteins.In addition,the accuracy and efficiency can be globally enhanced with BRD proteins binding to other loci in the chromatin histone.

关 键 词：BRD蛋白 染色质乙酰化 转录调控 

分 类 号：Q75[生物学—分子生物学]