Alexander R W, Schimmel P
Department of Chemistry, Wake Forest University, Winston-Salem, North Carolina 27109, USA.
Prog Nucleic Acid Res Mol Biol. 2001;69:317-49. doi: 10.1016/s0079-6603(01)69050-0.
Aminoacyl-tRNA synthetases are modular proteins, with domains that have distinct roles in the aminoacylation reaction. The catalytic core is responsible for aminoacyl adenylate formation and transfer of the amino acid to the 3' end of the bound transfer RNA (tRNA). Appended and inserted domains contact portions of the tRNA outside the acceptor site and contribute to the efficiency and specificity of aminoacylation. Some aminoacyl-tRNA synthetases also have distinct editing activities that are localized to unique domains. Efficient aminoacylation and editing require communication between RNA-binding and catalytic domains, and can be considered as a signal transduction system. Here, evidence for domain-domain communication in aminoacyl-tRNA synthetases is summarized, together with insights from structural analysis.
氨酰-tRNA合成酶是模块化蛋白质，其结构域在氨酰化反应中具有不同作用。催化核心负责氨酰腺苷酸的形成以及将氨基酸转移到结合的转运RNA（tRNA）的3'末端。附加和插入结构域与受体位点外的tRNA部分接触，并有助于提高氨酰化的效率和特异性。一些氨酰-tRNA合成酶还具有定位于独特结构域的独特校对活性。高效的氨酰化和校对需要RNA结合结构域和催化结构域之间的通讯，并且可以被视为一种信号转导系统。在此，总结了氨酰-tRNA合成酶中结构域-结构域通讯的证据，以及来自结构分析的见解。
