A type II toxin–antitoxin system is responsible for the cell death at low temperature in Pseudomonas syringae Lz4W lacking RNase R

• Published in: The Journal of biological chemistry Vol. 300; no. 8; p. 107600
• Main Authors: Mittal, Pragya, Sinha, Anurag K., Pandiyan, Apuratha, Kumari, Leela, Ray, Malay K., Pavankumar, Theetha L.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.08.2024; American Society for Biochemistry and Molecular Biology
• Subjects: cell death; cold sensitivity; cold-induced DNA damage; Collection: Microbiology; RNA degradation; RNA unwinding; toxin–antitoxin system; cell death; cold sensitivity; RNase REc; RNA unwinding; RNA degradation; toxin–antitoxin system; RNase RPs; TA; pLz4W; PFGE; cold-induced DNA damage; CSD; psA–psT; and Toxin-antitoxin system; Cold-sensitivity
• DOI: 10.1016/j.jbc.2024.107600
• ISSN: 0021-9258; 1083-351X

RNase R (encoded by the rnr gene) is a highly processive 3′ → 5′ exoribonuclease essential for the growth of the psychrotrophic bacterium Pseudomonas syringae Lz4W at low temperature. The cell death of a rnr deletion mutant at low temperature has been previously attributed to processing defects in 16S rRNA, defective ribosomal assembly, and inefficient protein synthesis. We recently showed that RNase R is required to protect P. syringae Lz4W from DNA damage and oxidative stress, independent of its exoribonuclease activity. Here, we show that the processing defect in 16S rRNA does not cause cell death of the rnr mutant of P. syringae at low temperature. Our results demonstrate that the rnr mutant of P. syringae Lz4W, complemented with a RNase R deficient in exoribonuclease function (RNase RD284A), is defective in 16S rRNA processing but can grow at 4 °C. This suggested that the processing defect in ribosomal RNAs is not a cause of the cold sensitivity of the rnr mutant. We further show that the rnr mutant accumulates copies of the indigenous plasmid pLz4W that bears a type II toxin–antitoxin (TA) system (P. syringae antitoxin–P. syringae toxin). This phenotype was rescued by overexpressing antitoxin psA in the rnr mutant, suggesting that activation of the type II TA system leads to cold sensitivity of the rnr mutant of P. syringae Lz4W. Here, we report a previously unknown functional relationship between the cold sensitivity of the rnr mutant and a type II TA system in P. syringae Lz4W.