4.8 Article

An ADP-ribosyltransferase toxin kills bacterial cells by modifying structured non-coding RNAs

期刊

MOLECULAR CELL
卷 82, 期 18, 页码 3484-+

出版社

CELL PRESS
DOI: 10.1016/j.molcel.2022.08.015

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资金

  1. Natural Sciences and Engineering Research Council of Canada (NSERC)
  2. Canadian Institutes of Health Research (CIHR) Fellowship
  3. Biotechnology and Biological Sciences Research Council
  4. Natural Sciences and Engineering Research Council (NSERC)
  5. National Research Council (NRC)
  6. Government of Saskatchewan
  7. University of Saskatchewan
  8. Medical Research Council [MR/S02316X/1]
  9. NSERC [RGPIN-2018-04968]
  10. CIHR [PJT-175011]
  11. Canada Foundation for Innovation (CFI)
  12. Canadian Institutes of Health Research (CIHR)
  13. Burroughs Wellcome Fund

向作者/读者索取更多资源

ADP-ribosyltransferases (ARTs) are bacterial virulence factors that modify essential proteins to promote pathogenesis. This study reports the discovery of RhsP2 as an ART toxin delivered by a type VI secretion system. RhsP2 can ADP-ribosylate double-stranded RNA, leading to inhibition of translation and disruption of tRNA processing, ultimately causing cell death. This finding uncovers a previously unknown mechanism of bacterial antagonism and highlights the unprecedented activity of ART enzymes.
ADP-ribosyltransferases (ARTs) were among the first identified bacterial virulence factors. Canonical ART toxins are delivered into host cells where they modify essential proteins, thereby inactivating cellular pro-cesses and promoting pathogenesis. Our understanding of ARTs has since expanded beyond protein -target-ing toxins to include antibiotic inactivation and DNA damage repair. Here, we report the discovery of RhsP2 as an ART toxin delivered between competing bacteria by a type VI secretion system of Pseudomonas aer-uginosa. A structure of RhsP2 reveals that it resembles protein-targeting ARTs such as diphtheria toxin. Remarkably, however, RhsP2 ADP-ribosylates 20-hydroxyl groups of double-stranded RNA, and thus, its ac-tivity is highly promiscuous with identified cellular targets including the tRNA pool and the RNA-processing ribozyme, ribonuclease P. Consequently, cell death arises from the inhibition of translation and disruption of tRNA processing. Overall, our data demonstrate a previously undescribed mechanism of bacterial antago-nism and uncover an unprecedented activity catalyzed by ART enzymes.

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