Structure of the MazF-mt9 toxin, a tRNA-specific endonuclease from Mycobacterium tuberculosis

被引：13

作者：

Chen, Ran ^{[1
]}

Tu, Jie ^{[1
]}

Liu, Zhihui ^{[2
]}

Meng, Fanrong ^{[2
]}

Ma, Pinyun ^{[2
]}

Ding, Zhishan ^{[1
]}

Yang, Chengwen ^{[1
]}

Chen, Lei ^{[1
]}

Deng, Xiangyu ^{[1
]}

Xie, Wei ^{[1
]}

机构：

[1] Sun Yat Sen Univ, Sch Life Sci, State Key Lab Biocontrol, 135 Xingang Rd, Guangzhou 510275, Guangdong, Peoples R China

[2] Guangzhou Chest Hosp, 62 HengzhiGang Rd, Guangzhou 510095, Guangdong, Peoples R China

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2017年 / 486卷 / 03期

关键词：

Crystal structure; Toxin-antitoxin; tRNA endonuclease; Structure-function; Substrate specificity; ANTITOXIN SYSTEMS; CYTOTOXIC RIBONUCLEASE; ESCHERICHIA-COLI; CLEAVAGE; RECOGNITION; VIRULENCE; COMPLEX;

D O I：

10.1016/j.bbrc.2017.03.132

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：

Tuberculosis (TB) is a severe disease caused by Mycobacterium tuberculosis (M. tb) and the well characterized M. tb MazE/F proteins play important roles in stress adaptation. Recently, the MazF-mt9 toxin has been found to display endonuclease activities towards tRNAs but the mechanism is unknown. We hereby present the crystal structure of apo-MazF-mt9. The enzyme recognizes tRNALYs with a central UUU motif within the anticodon loop, but is insensitive to the sequence context outside of the loop. Based on our crystallographic and biochemical studies, we identified key residues for catalysis and proposed the potential tRNA-binding site. (C) 2017 Elsevier Inc. All rights reserved.

引用

页码：804 / 810

页数：7

共 18 条

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