第一类肽链释放因子结构与功能研究的新进展  

New Progress in Function and Structure of The Class Ⅰ Polypeptide Release Factors

作　　者：陈洁[1] 柴宝峰[1] 梁爱华[1] 

机构地区：[1]化学生物学和分子工程教育部重点实验室,山西大学生物技术研究所,太原030006

出　　处：《生物化学与生物物理进展》2009年第7期817-822,共6页Progress In Biochemistry and Biophysics

基　　金：国家自然科学基金资助项目(30670282,30770294)~~

摘　　要：蛋白质生物合成过程的终止是由于第一类肽链释放因子识别终止密码子,并导致肽酰-tRNA酯键水解,释放出新合成的多肽链.近期,通过冷冻电镜、结晶学、核磁共振、分子动力学和生物化学等方面的研究,使第一类肽链释放因子的结构与功能逐渐清晰.对近期的研究进行了分析和整理.The process of protein synthesis is terminated by one of the three stop codons which are recognized by class Ⅰ polypeptide release factors. Subsequently, it could promote the hydrolysis of the ester bond of peptidy-tRNA, resulting in release of the nascent polypeptide. Recent results from cryoelectron microscopy, crystallography, NMR, molecular dynamic and biochemical experiments have shed considerable light on the function and structure of the class Ⅰ release factors. The progress in these aspects were summarized.

关 键 词：第一类肽链释放因子 冷冻电镜 晶体结构 核磁共振 分子动力学 

分 类 号：Q753[生物学—分子生物学]