Aminoacylation of tRNA 2 '- or 3 '-hydroxyl by phosphoseryl- and pyrrolysyl-tRNA synthetases

作者：Englert Markus; Moses Sarath; Hohn Michael; Ling Jiqiang; O'Donoghue Patrick; Soell Dieter

来源：FEBS Letters, 2013, 587(20): 3360-3364.

DOI：10.1016/j.febslet.2013.08.037

• Protein synthesis
• tRNA esterification
• Amino acid

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.

• 出版日期2013-10-11