%0 Journal Article
%T Adaptation of a eukaryote-like ProRS to a prokaryote-like tRNAPro.
%A Ivanesthi IR
%A Latifah E
%A Amrullah LF
%A Tseng YK
%A Chuang TH
%A Pan HC
%A Yang CS
%A Liu SY
%A Wang CC
%J Nucleic Acids Res
%V 52
%N 12
%D 2024 Jul 8
%M 38842939
%F 19.16
%R 10.1093/nar/gkae483
%X Prolyl-tRNA synthetases (ProRSs) are unique among aminoacyl-tRNA synthetases (aaRSs) in having two distinct structural architectures across different organisms: prokaryote-like (P-type) and eukaryote/archaeon-like (E-type). Interestingly, Bacillus thuringiensis harbors both types, with P-type (BtProRS1) and E-type ProRS (BtProRS2) coexisting. Despite their differences, both enzymes are constitutively expressed and functional in vivo. Similar to BtProRS1, BtProRS2 selectively charges the P-type tRNAPro and displays higher halofuginone tolerance than canonical E-type ProRS. However, these two isozymes recognize the primary identity elements of the P-type tRNAPro-G72 and A73 in the acceptor stem-through distinct mechanisms. Moreover, BtProRS2 exhibits significantly higher tolerance to stresses (such as heat, hydrogen peroxide, and dithiothreitol) than BtProRS1 does. This study underscores how an E-type ProRS adapts to a P-type tRNAPro and how it may contribute to the bacterium's survival under stress conditions.