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• W1572562143 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." @default.
• W1572562143 created "2016-06-24" @default.
• W1572562143 creator A5029945783 @default.
• W1572562143 creator A5052614042 @default.
• W1572562143 date "2003-01-13" @default.
• W1572562143 modified "2023-10-17" @default.
• W1572562143 title "tmRNA from Thermus thermophilus. Interaction with alanyl-tRNA synthetase and elongation factor Tu" @default.
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• W1572562143 doi "https://doi.org/10.1046/j.1432-1033.2003.03401.x" @default.
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