Crystal Structure Analyses of Selenoprotein Biosynthesis

硒蛋白生物合成的晶体结构分析

• 批准号: 5241252
• 负责人: Professor Dr. Markus C. Wahl
• 金额: --
• 依托单位: Arbeitsgruppe Strukturbiochemie
• 依托单位国家: 德国
• 项目类别: Priority Programmes
• 财政年份: 2000
• 资助国家: 德国
• 起止时间: 1999-12-31 至 2007-12-31
• 项目状态: 已结题
• 来源: https://gepris.dfg.de/gepris/projekt/5241252?language=en
• 关键词: Crystal; Structure; Analyses; Selenoprotein; Biosynthesis

Crystal structures of protein and RNA components involved in the biosynthesis of selenocysteine and its cotranslational incorporation into selenoproteins in the Archaeon Methanococcus jannaschii and the Bacterium Eubacterium acidaminophilum shall be determined. The pertaining factors are selenocysteine synthase (SelA), elongation factor SelB, tRNASec (SelC), seryltRNA synthetase (SerRS), and selenophosphate synthetase (SelD). Aims of the projects are to explore the mechanistics of selenocysteine synthesis by SelA, to elucidate the structural peculiarities of the selenocysteine specific tRNASec, to understand its discrimination by seryl-tRNA synthetase, by selenocysteine synthase, and by elongation factor SelB, to structurally clarify the interactions of SelB with mRNA SECIS-elements, and to explain the mechanism of synthesis of the activated selenium donor, selenophosphate, by selenophosphate synthetase. The structures shall aid in understanding the mechanisms of this unique expansion of the genetic code and in characterizing the corresponding systems in higher organisms.

在jannaschii太古菌Methanococcus jannaschii和嗜酸嗜氨真杆菌（Eubacterium acidaminophilum）中，参与硒氨酸半胱氨酸生物合成的蛋白质和RNA组分的晶体结构及其与硒蛋白的共翻译结合将被确定。相关因子为硒代半胱氨酸合成酶（SelA）、延伸因子SelB、tRNASec （SelC）、seryltRNA合成酶（SerRS）和硒代磷酸合成酶（SelD）。本项目的目的是探讨SelA合成硒半胱氨酸的机制，阐明硒半胱氨酸特异性tRNASec的结构特点，了解seryl-tRNA合成酶、硒半胱氨酸合成酶和延伸因子SelB对其的区分，从结构上阐明SelB与mRNA secis元件的相互作用，并解释硒磷酸合成酶合成活化硒供体硒磷酸的机制。这些结构将有助于理解这种独特的遗传密码扩展的机制，并有助于描述高等生物中相应系统的特征。