Studying base pair open-close kinetics of tRNALeu by TROSY-based proton exchange NMR spectroscopy

Zhan-Xi Hao; Min Tan; Chang-Dong Liu; Rui Feng; En-Duo Wang; Guang Zhu

doi:10.1016/j.febslet.2010.10.002

Studying base pair open-close kinetics of tRNALeu by TROSY-based proton exchange NMR spectroscopy

FEBS Lett. 2010 Nov 5;584(21):4449-52. doi: 10.1016/j.febslet.2010.10.002. Epub 2010 Oct 13.

Authors

Zhan-Xi Hao¹, Min Tan, Chang-Dong Liu, Rui Feng, En-Duo Wang, Guang Zhu

Affiliation

¹ State Key Laboratory of Molecular Biology, Shanghai Institutes for Biological Sciences, Graduate School of the Chinese Academy of Sciences, The Chinese Academy of Sciences, Shanghai, China.

PMID: 20937276
DOI: 10.1016/j.febslet.2010.10.002

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 tRNA(Leu) (CAG), and their dependence on magnesium ion concentration. Finally, we correlated millisecond conformational flexibility with aminoacylation of tRNA(Leu) and proposed that the flexibility of the acceptor stem and the core region might contribute to aminoacylation of tRNA(Leu).

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Aminoacylation
Base Pairing*
Base Sequence
Escherichia coli
Kinetics
Magnetic Resonance Spectroscopy / methods*
Protons*
RNA, Bacterial / chemistry
RNA, Bacterial / genetics
RNA, Bacterial / metabolism
RNA, Transfer / chemistry*
RNA, Transfer / genetics
RNA, Transfer / metabolism

Substances

Protons
RNA, Bacterial
RNA, Transfer