RtcB2‐PrfH Operon Protects E. coli ATCC25992 Strain from Colicin E3 Toxin

Tinashe P. Maviza, Anastasiia S. Zarechenskaia, Nadezhda R. Burmistrova, Andrey S. Tchoub, Olga A. Dontsova, Petr V. Sergiev, Ilya A. Osterman

Research output: Contribution to journalArticlepeer-review


In the bid to survive and thrive in an environmental setting, bacterial species constantly interact and compete for resources and space in the microbial ecosystem. Thus, they have adapted to use various antibiotics and toxins to fight their rivals. Simultaneously, they have evolved an abil-ity to withstand weapons that are directed against them. Several bacteria harbor colicinogenic plas-mids which encode toxins that impair the translational apparatus. One of them, colicin E3 ribotoxin, mediates cleavage of the 16S rRNA in the decoding center of the ribosome. In order to thrive upon deployment of such ribotoxins, competing bacteria may have evolved counter‐conflict mechanisms to prevent their demise. A recent study demonstrated the role of PrfH and the RtcB2 module in rescuing a damaged ribosome and the subsequent re‐ligation of the cleaved 16S rRNA by colicin E3 in vitro. The rtcB2‐prfH genes coexist as gene neighbors in an operon that is sporadically spread among different bacteria. In the current study, we report that the RtcB2‐PrfH module confers resistance to colicin E3 toxicity in E. coli ATCC25922 cells in vivo. We demonstrated that the viability of E. coli ATCC25922 strain that is devoid of rtcB2 and prfH genes is impaired upon action of colicin E3, in contrast to the parental strain which has intact rtcB2 and prfH genes. Complementation of the rtcB2 and prfH gene knockout with a high copy number‐plasmid (encoding either rtcB2 alone or both rtcB2‐prfH operon) restored resistance to colicin E3. These results highlight a counter‐conflict system that may have evolved to thwart colicin E3 activity.

Original languageEnglish
Article number6453
JournalInternational Journal of Molecular Sciences
Issue number12
Publication statusPublished - 1 Jun 2022


  • bacteria
  • ribosome rescue
  • RNA ligation
  • rRNA cleavage
  • translation
  • translation termination factor


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