Structural Investigations of RNA-Protein Complexes in Post-Ribosomal Era

被引：1

作者：

Tishchenko, S. V. ^{[1
]}

Mikhailina, A. O. ^{[1
]}

Lekontseva, N. V. ^{[1
]}

Stolboushkina, E. A. ^{[1
]}

Nikonova, E. Yu. ^{[1
]}

Nikonov, O. S. ^{[1
]}

Nikulin, A. D. ^{[1
]}

机构：

[1] Russian Acad Sci, Inst Prot Res, Pushchino 142290, Moscow Oblast, Russia

来源：

CRYSTALLOGRAPHY REPORTS | 2021年 / 66卷 / 05期

基金：

俄罗斯科学基金会; 俄罗斯基础研究基金会;

关键词：

INITIATION-FACTOR; 2; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; METHANOCOCCUS-VANNIELII; BINDING PROPERTIES; MESSENGER-RNA; MVAL1; OPERON; DOMAIN-I; HFQ; TRANSLATION;

D O I：

10.1134/S1063774521050217

中图分类号：

O7 [晶体学];

学科分类号：

0702 ; 070205 ; 0703 ; 080501 ;

摘要：

Structural studies of RNA-protein complexes are important for understanding many molecular mechanisms occurring in cells (e.g., regulation of protein synthesis and RNA-chaperone activity of proteins). Various objects investigated at the Institute of Protein Research of the Russian Academy of Sciences are considered. Based on the analysis of the structures of the complexes of the ribosomal protein L1 with specific regions on both mRNA and rRNA, the principles of regulation of the translation of the mRNA of its own operon are presented. The studies of the heterotrimeric translation initiation factor IF2 of archaea and eukaryotes are described, and the data on the interaction of glycyl-tRNA-synthetase with viral IRES are reported. The results of studying the interaction of RNA molecules with one of functionally important sites of the Hfq protein are presented, and the differences in the RNA-binding properties of the Hfq and archaeal Lsm proteins are revealed.

引用

页码：726 / 736

页数：11