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• W2003421765 abstract "Class I and II aminoacyl-tRNA synthetases (AARSs) attach amino acids to the 2'- and 3'-OH of the tRNA terminal adenosine, respectively. One exception is phenylalanyl-tRNA synthetase (PheRS), which belongs to Class II but attaches phenylalanine to the 2'-OH. Here we show that two Class II AARSs, O-phosphoseryl- (SepRS) and pyrrolysyl-tRNA (PylRS) synthetases, aminoacylate the 2'- and 3'-OH, respectively. Structure-based-phylogenetic analysis reveals that SepRS is more closely related to PheRS than PylRS, suggesting that the idiosyncratic feature of 2'-OH acylation evolved after the split between PheRS and PylRS. Our work completes the understanding of tRNA aminoacylation positions for the 22 natural AARSs." @default.
• W2003421765 created "2016-06-24" @default.
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• W2003421765 date "2013-09-07" @default.
• W2003421765 modified "2023-09-26" @default.
• W2003421765 title "Aminoacylation of tRNA 2′- or 3′-hydroxyl by phosphoseryl- and pyrrolysyl-tRNA synthetases" @default.
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• W2003421765 doi "https://doi.org/10.1016/j.febslet.2013.08.037" @default.
• W2003421765 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3830498" @default.
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• W2003421765 hasPublicationYear "2013" @default.
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