Backbone and side-chain resonance assignments for the tmRNA-binding protein,SmpB, from <Emphasis Type="Italic">Mycobacterium tuberculosis</Emphasis> |
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| Authors: | Juanjuan Yang Yindi Liu Zhao Liu Chun Meng Donghai Lin |
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| Institution: | 1.Institute of Pharmaceutical Biotechnology and Engineering, College of Biological Science and Biotechnology,Fuzhou University,Fuzhou,China;2.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,China |
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| Abstract: | 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 1H, 13C and 15N 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. |
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