FEBS Letters | |
Fluorine‐19 NMR studies of the thermal unfolding of 5‐fluorouracil‐substituted Escherichia coli valine transfer RNA | |
Chu, Wen-Chy1  Horowitz, Jack1  | |
[1] Department of Biochemistry and Biophysics, Iowa State University, Ames, Iowa 50011, USA | |
关键词: 19F NMR; Fluorouracil; Transfer RNA; Thermal unfolding; Escherichia coli; NMR; nuclear magnetic resonance; FUra; 5-fluorouracil; (FUra)tRNAVal; 5-fluorouracil-substituted E. coli tRNAVal; | |
DOI : 10.1016/0014-5793(91)81408-Z | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
19F NMR spectroscopy was used to monitor the thermal unfolding of E. coli tRNAVal labeled by incorporation of 5-fluorouracil (FUra). With rising temperatures, resonances in the 19F NMR spectrum of (FUra)tRNAVal gradually shift towards the central region of the spectrum and merge into a single broad peak above 85°C. FU55 and FU12 are the first to shift, beginning at temperatures below 40°C, which suggests that the initial steps of thermal denaturation of tRNAVal involve disruption of the tertiary interactions between the D- and T-arms. The acceptor stem and the FU64-G50 wobble base pair in the T-stem are particularly stable to thermal denaturation. A temperature-dependent splitting of the 19F resonance assigned to FU64, at temperatures above 40°C, suggests that the T-arm of (FUra)tRNAVal exists in two conformations in slow exchange on the NMR time scale.
【 授权许可】
Unknown
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