Prophage terminase with tRNase activity sensitizes Salmonella enterica to oxidative stress

• 成果类型: Article
• 署名作者: Uppalapati, Siva; Kant, Sashi; Liu, Lin; Kim, Ju-Sim; Orlicky, David; Mcclelland, Michael; Vazquez-Torres, Andres
• 署名单位: University of Colorado System; University of Colorado Anschutz Medical Campus; University of Colorado System; University of Colorado Anschutz Medical Campus; University of California System; University of California Irvine
• 刊物名称: SCIENCE
• ISSN/ISSBN: 0036-10202
• DOI: 10.1126/science.adl3222
• 发表日期: 2024-04-05
• 页码: 100-105
• 关键词: ligase rtcb; rna; bacteriophage; ribosome; oxidase; repair; fate

摘要

Phage viruses shape the evolution and virulence of their bacterial hosts. The Salmonella enterica 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 tRNALeu. The ensuing RNA fragmentation compromises bacterial translation, intracellular survival, and recovery from oxidative stress in the vertebrate host. S. enterica 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.