Prophage terminase with tRNase activity sensitizes <i>Salmonella enterica</i> to oxidative stress.
basic_science · Level V
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- Record sourced from PubMed, PMID 38574144.
- Also identified by DOI 10.1126/science.adl3222 and PMC identifier 11443816.
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Abstract
Phage viruses shape the evolution and virulence of their bacterial hosts. The <i>Salmonella enterica</i> genome encodes several stress-inducible prophages. The Gifsy-1 prophage terminase protein, whose canonical function is to process phage DNA for packaging in the virus head, unexpectedly acts as a transfer ribonuclease (tRNase) under oxidative stress, cleaving the anticodon loop of tRNA<sup>Leu</sup>. The ensuing RNA fragmentation compromises bacterial translation, intracellular survival, and recovery from oxidative stress in the vertebrate host. <i>S. enterica</i> adapts to this transfer RNA (tRNA) fragmentation by transcribing the RNA repair Rtc system. The counterintuitive translational arrest provided by tRNA cleavage may subvert prophage mobilization and give the host an opportunity for repair as a way of maintaining bacterial genome integrity and ultimately survival in animals.
Medical subject headings
- Endodeoxyribonucleases
- Prophages
- Salmonella enterica
- Salmonella Phages
- Viral Proteins