| Literature DB >> 12542696 |
Victor G Stepanov1, Jens Nyborg.
Abstract
The interaction of a Thermus thermophilus tmRNA transcript with alanyl-tRNA synthetase and elongation factor Tu has been studied. The synthetic tmRNA was found to be stable up to 70 degrees C. The thermal optimum of tmRNA alanylation was determined to be around 50 degrees C. At 50 degrees C, tmRNA transcript was aminoacylated by alanyl-tRNA synthetase with 5.9 times lower efficiency (kcat/Km) than tRNAAla, primarily because of the difference in turnover numbers (kcat). Studies on EF-Tu protection of Ala approximately tmRNA against alkaline hydrolysis revealed the existence of at least two different binding sites for EF-Tu on charged tmRNA. The possible nature of these binding sites is discussed.Entities:
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Year: 2003 PMID： 12542696 DOI： 10.1046/j.1432-1033.2003.03401.x
Source DB: PubMed Journal: Eur J Biochem ISSN： 0014-2956