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• W2108465110 endingPage "82" @default.
• W2108465110 startingPage "73" @default.
• W2108465110 abstract "The GTP-bound form of elongation factor Tu (EF-Tu) brings aminoacylated tRNAs (aa-tRNA) to the A-site of the ribosome. EF-Tu binds all cognate elongator aa-tRNAs with highly similar affinities, and its weaker or tighter binding of misacylated tRNAs may discourage their participation in translation. Norvaline (Nva) is a non-proteinogenic amino acid that is activated and transferred to tRNALeu by leucyl-tRNA synthetase (LeuRS). No notable accumulation of Nva-tRNALeu has been observed in vitro, because of the efficient post-transfer hydrolytic editing activity of LeuRS. However, incorporation of norvaline into proteins in place of leucine does occur under certain conditions in vivo. Here we show that EF-Tu binds Nva-tRNALeu and Leu-tRNALeu with similar affinities, and that Nva-tRNALeu and Leu-tRNALeu dissociate from EF-Tu at comparable rates. The inability of EF-Tu to discriminate against norvaline may have driven evolution of highly efficient LeuRS editing as the main quality control mechanism against misincorporation of norvaline into proteins." @default.
• W2108465110 created "2016-06-24" @default.
• W2108465110 creator A5006320247 @default.
• W2108465110 creator A5042181382 @default.
• W2108465110 creator A5073389988 @default.
• W2108465110 date "2013-01-01" @default.
• W2108465110 modified "2023-10-16" @default.
• W2108465110 title "Lack of Discrimination Against Non-proteinogenic Amino Acid Norvaline by Elongation Factor Tu from Escherichia coli" @default.
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• W2108465110 doi "https://doi.org/10.5562/cca2173" @default.
• W2108465110 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3675784" @default.
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• W2108465110 hasPublicationYear "2013" @default.
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