Adaptation of a eukaryote-like ProRS to a prokaryote-like tRNAPro.
Nucleic Acids Res
; 52(12): 7158-7170, 2024 Jul 08.
Article
in En
| MEDLINE
| ID: mdl-38842939
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Bacillus thuringiensis
/
Amino Acyl-tRNA Synthetases
Language:
En
Journal:
Nucleic Acids Res
Year:
2024
Document type:
Article
Affiliation country:
Taiwán