结核分枝杆菌中一种tRNA特异性核酸内切酶MazF-mt9毒素的结构
Structure of the MazF-mt9 toxin, a tRNA-specific endonuclease from Mycobacterium tuberculosis.
作者信息
Chen Ran, Tu Jie, Liu Zhihui, Meng Fanrong, Ma Pinyun, Ding Zhishan, Yang Chengwen, Chen Lei, Deng Xiangyu, Xie Wei
机构信息
State Key Laboratory for Biocontrol, School of Life Sciences, The Sun Yat-Sen University, 135 W. Xingang Rd., Guangzhou, Guangdong 510275, People's Republic of China.
Guangzhou Chest Hospital, 62 HengzhiGang Rd., Guangzhou, Guangdong 510095, People's Republic of China.
出版信息
Biochem Biophys Res Commun. 2017 May 6;486(3):804-810. doi: 10.1016/j.bbrc.2017.03.132. Epub 2017 Mar 25.
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 tRNA 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.
结核病（TB）是由结核分枝杆菌（M. tb）引起的一种严重疾病，且特征明确的M. tb MazE/F蛋白在应激适应中发挥重要作用。最近，已发现MazF-mt9毒素对tRNA具有核酸内切酶活性，但其机制尚不清楚。我们在此展示了脱辅基MazF-mt9的晶体结构。该酶识别反密码子环内具有中央UUU基序的tRNA，但对环外的序列背景不敏感。基于我们的晶体学和生化研究，我们确定了催化的关键残基并提出了潜在的tRNA结合位点。
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