{Reference Type}: Journal Article
{Title}: Adaptation of a eukaryote-like ProRS to a prokaryote-like tRNAPro.
{Author}: Ivanesthi IR;Latifah E;Amrullah LF;Tseng YK;Chuang TH;Pan HC;Yang CS;Liu SY;Wang CC;
{Journal}: Nucleic Acids Res
{Volume}: 52
{Issue}: 12
{Year}: 2024 Jul 8
{Factor}: 19.16
{DOI}: 10.1093/nar/gkae483
{Abstract}: 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.