PMID:11743004
| Citation |
Mansell, JB, Guévremont, D, Poole, ES and Tate, WP (2001) A dynamic competition between release factor 2 and the tRNA(Sec) decoding UGA at the recoding site of Escherichia coli formate dehydrogenase H. EMBO J. 20:7284-93 |
|---|---|
| Abstract |
Factors affecting competition between termination and elongation in vivo during translation of the fdhF selenocysteine recoding site (UGA) were studied with wild-type and modified fdhF sequences. Altering sequences surrounding the recoding site UGA without affecting RNA secondary structure indicated that the kinetics of stop signal decoding have a significant influence on selenocysteine incorporation efficiency. The UGA in the wild-type fdhF sequence remains 'visible' to the factor and forms a site-directed cross-link when mRNA stem-loop secondary structure is absent, but not when it is present. The timing of the secondary structure unfolding during translation may be a critical feature of competition between release factor 2 and tRNA(Sec) for decoding UGA. Increasing the cellular concentration of either of these decoding molecules for termination or selenocysteine incorporation showed that they were able to compete for UGA by a kinetic competition that is dynamic and dependent on the Escherichia coli growth rate. The tRNA(Sec)-mediated decoding can compete more effectively for the UGA recoding site at lower growth rates, consistent with anaerobic induction of fdhF expression. |
| Links |
PubMed PMC125778 Online version:10.1093/emboj/20.24.7284 |
| Keywords |
Base Sequence; Escherichia coli/enzymology; Formate Dehydrogenases/genetics; Hydrogenase/genetics; Molecular Sequence Data; Multienzyme Complexes/genetics; Nucleic Acid Conformation; Peptide Termination Factors/metabolism; Protein Biosynthesis; RNA, Transfer, Amino Acid-Specific/chemistry; RNA, Transfer, Amino Acid-Specific/genetics; RNA, Transfer, Amino Acid-Specific/metabolism |
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