國家衛生研究院 NHRI:Item 3990099045/15897
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    Please use this identifier to cite or link to this item: http://ir.nhri.org.tw/handle/3990099045/15897


    Title: Adaptation of a eukaryote-like ProRS to a prokaryote-like tRNApro
    Authors: Ivanesthi, IR;Latifah, E;Amrullah, LF;Tseng, YK;Chuang, TH;Pan, HC;Yang, CS;Liu, SY;Wang, CC
    Contributors: Immunology Research Center
    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 tRNA(Pro) and displays higher halofuginone tolerance than canonical E-type ProRS. However, these two isozymes recognize the primary identity elements of the P-type tRNA(Pro)& horbar;G72 and A73 in the acceptor stem & horbar;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 tRNA(Pro) and how it may contribute to the bacterium's survival under stress conditions.
    Date: 2024-07-08
    Relation: Nucleic Acids Research. 2024 Jul 08;52(12):7158-7170.
    Link to: http://dx.doi.org/10.1093/nar/gkae483
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=0305-1048&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:001240097300001
    Cited Times(Scopus): https://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85197968749
    Appears in Collections:[Tsung-Hsien Chuang] Periodical Articles

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