Crystal structure of Nanoarchaeum equitans tyrosyl-tRNA synthetase and its aminoacylation activity toward tRNATyr with an extra guanosine residue at the 5′-terminus

被引:1
|
作者
Horikoshi, Tatsuya [1 ]
Noguchi, Hiroki [2 ]
Umehara, Takuya [1 ]
Mutsuro-Aoki, Hiromi [1 ]
Kurihara, Ryodai [1 ]
Noguchi, Ryohei [1 ]
Hashimoto, Takahiro [1 ]
Watanabe, Yuki [1 ]
Ando, Tadashi [3 ,4 ]
Kamata, Kenichi [2 ]
Park, Sam-Yong [2 ]
Tamura, Koji [1 ,4 ]
机构
[1] Tokyo Univ Sci, Dept Biol Sci & Technol, Katsushika Ku, 6-3-1 Niijuku, Tokyo 1258585, Japan
[2] Yokohama City Univ, Grad Sch Med Life Sci, Drug Design Lab, Tsurumi Ku, Yokohama, Kanagawa 2300045, Japan
[3] Tokyo Univ Sci, Dept Appl Elect, Katsushika Ku, 6-3-1 Niijuku, Tokyo 1258585, Japan
[4] Tokyo Univ Sci, Res Inst Sci & Technol, 2641 Yamazaki, Noda, Chiba 2788510, Japan
基金
日本学术振兴会;
关键词
tRNA; Tyrosyl-tRNA synthetase; Nanoarchaeum equitans; Crystal structure; Aminoacylation; Extra guanosine residue at the 5 '-terminus; CHIRAL-SELECTIVE AMINOACYLATION; SACCHAROMYCES-CEREVISIAE; RIBONUCLEASE-P; POLYMERASE; EVOLUTION; IDENTITY; FEATURES; MOTIFS; DOMAIN; GENES;
D O I
10.1016/j.bbrc.2021.08.070
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
tRNA(Tyr) of Nanoarchaeum equitans has a remarkable feature with an extra guanosine residue at the 5' terminus. However, the N. equitans tRNA(Tyr) mutant without extra guanosine at the 5'-end was tyrosylated by tyrosyl-tRNA synthase (TyrRS). We solved the crystal structure of N. equitans TyrRS at 2.80 A resolution. By comparing the present solved structure with the complex structures TyrRS with tRNATyr of Thermus thermophilus and Methanocaldococcus jannaschii, an arginine substitution mutant of N. equitans TyrRS at Ile200 (I200R), which is the putative closest candidate to the 5'-phosphate of C1 of N. equitans tRNA(Tyr), was prepared. The I200R mutant tyrosylated not only wild-type tRNA(Tyr) but also the tRNA without the G-1 residue. Further tyrosylation analysis revealed that the second base of the anticodon (U35), discriminator base (A73), and C1:G72 base pair are strong recognition sites. (C) 2021 Published by Elsevier Inc.
引用
收藏
页码:90 / 95
页数:6
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