Adaptation of a eukaryote-like ProRS to a prokaryote-like tRNAPro

Indira Rizqita Ivanesthi, Emi Latifah, Luqman Fikri Amrullah, Yi Kuan Tseng, Tsung Hsien Chuang, Hung Chuan Pan, Chih Shiang Yang, Shih Yang Liu, Chien Chia Wang

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

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.

Original languageEnglish
Pages (from-to)7158-7170
Number of pages13
JournalNucleic Acids Research
Volume52
Issue number12
DOIs
StatePublished - 8 Jul 2024

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