Ancestral AlaX editing enzymes for control of genetic code fidelity are not tRNA-specific.

The Journal of Biological Chemistry
Eva Maria NovoaLluís Ribas de Pouplana

Abstract

Accurate protein synthesis requires the hydrolytic editing of tRNAs incorrectly aminoacylated by aminoacyl-tRNA synthetases (ARSs). Recognition of cognate tRNAs by ARS is less error-prone than amino acid recognition, and, consequently, editing domains are generally believed to act only on the tRNAs cognate to their related ARSs. For example, the AlaX family of editing domains, including the editing domain of alanyl-tRNA synthetase and the related free-standing trans-editing AlaX enzymes, are thought to specifically act on tRNA(Ala), whereas the editing domains of threonyl-tRNA synthetases are specific for tRNA(Thr). Here we show that, contrary to this belief, AlaX-S, the smallest of the extant AlaX enzymes, deacylates Ser-tRNA(Thr) in addition to Ser-tRNA(Ala) and that a single residue is important to determine this behavior. Our data indicate that promiscuous forms of AlaX are ancestral to tRNA-specific AlaXs. We propose that former AlaX domains were used to maintain translational fidelity in earlier stages of genetic code evolution when mis-serylation of several tRNAs was possible.

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Citations

Aug 5, 2017·Proceedings of the National Academy of Sciences of the United States of America·Eric M DanhartKarin Musier-Forsyth
Feb 28, 2016·The Journal of Biological Chemistry·Nevena CvetesicIta Gruic-Sovulj
Mar 23, 2017·Biochimica Et Biophysica Acta. General Subjects·Noah M ReynoldsAna Crnković
May 26, 2016·EcoSal Plus·Richard Giegé, Mathias Springer
Sep 10, 2021·Nucleic Acids Research·Hong ZhangJiqiang Ling

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