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Studying base pair open-close kinetics of tRNALeu by TROSY-based proton exchange NMR spectroscopy |
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| Authors: | Hao Zhan-Xi Tan Min Liu Chang-Dong Feng Rui Wang En-Duo Zhu Guang |
| Institution: | a State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Graduate School of the Chinese Academy of Sciences, The Chinese Academy of Sciences, 320 Yueyang Road, Shanghai 200031, China b Division of Life Science, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China |
| Abstract: | The millisecond conformational flexibility is functionally important for nucleic acids and can be studied through probing the base pair open-close kinetics by proton exchange nuclear magnetic resonance (NMR) spectroscopy. Here, the traditional imino proton exchange NMR experiments were modified with transverse relaxation optimized spectroscopy and were applied to accurately measure imino proton exchange rates of all base pairs in Escherichia coli tRNALeu (CAG), and their dependence on magnesium ion concentration. Finally, we correlated millisecond conformational flexibility with aminoacylation of tRNALeu and proposed that the flexibility of the acceptor stem and the core region might contribute to aminoacylation of tRNALeu. |
| Keywords: | tRNA transfer ribonucleic acid aaRSs aminoacyl-tRNA synthetase LeuRS leucyl-tRNA synthetase NMR nuclear magnetic resonance TROSY transverse relaxation optimized spectroscopy HM(S)QC heteronuclear multiple(single) quantum correlation kex imino proton exchange rates Ec Escherichia coli |
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