Yang Juanjuan, Liu Yindi, Liu Zhao, Meng Chun, Lin Donghai
Institute of Pharmaceutical Biotechnology and Engineering, College of Biological Science and Biotechnology, Fuzhou University, Fuzhou, Fujian, 350108, China.
MOE Key Laboratory of Spectrochemical Analysis and Instrumentation, Key Laboratory for Chemical Biology of Fujian Province, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen, 361005, China.
Biomol NMR Assign. 2017 Oct;11(2):175-179. doi: 10.1007/s12104-017-9742-y. Epub 2017 Mar 4.
Small protein B (SmpB) is an essential molecule in trans-translation which is a universal biological pathway for protein synthesis in bacteria. Trans-translation can release stalled ribosomes from defective mRNAs and target tag-protein fragments for degradation, and then restart protein synthesis. The SmpB-tmRNA complex coordinating with other components of the trans-translation system, plays vital roles in Mycobacterium tuberculosis under both stress conditions and non-replicating conditions. Thus, elucidation of molecular details and dynamic properties of the SmpB-tmRNA interaction is a crucial step towards effectively blocking trans-translation process to shorten the duration of tuberculosis treatment. Here, we report resonance assignments for H, C and N of M. tuberculosis SmpB (MtSmpB, spanning residues 4-133) protein determined by a suite of 2D/3D heteronuclear NMR experiments along with predicted the secondary structure.
小蛋白B（SmpB）是反式翻译过程中的一种必需分子，反式翻译是细菌中蛋白质合成的普遍生物学途径。反式翻译可以从有缺陷的mRNA中释放停滞的核糖体，并将标记蛋白片段靶向降解，然后重新启动蛋白质合成。SmpB-tmRNA复合物与反式翻译系统的其他组分协同作用，在应激条件和非复制条件下的结核分枝杆菌中都起着至关重要的作用。因此，阐明SmpB-tmRNA相互作用的分子细节和动态特性是有效阻断反式翻译过程以缩短结核病治疗疗程的关键一步。在此，我们报告了通过一系列二维/三维异核核磁共振实验确定的结核分枝杆菌SmpB（MtSmpB，涵盖第4至133位残基）蛋白的氢、碳和氮的共振归属，并预测了其二级结构。
