Kinetics of P22 early gene expression suggests a cro-like regulatory function

Harvey, A. M.; Prell, Hermann H.

doi:10.1007/bf00271212

Cited by 3 publications

(1 citation statement)

References 35 publications

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“…Then eight Cro-like proteins in different bacteria were selected and aligned, and highly conserved amino acid sites were obtained ( Figure 5B ). In temperate phages, such as lambda and P22 phages, Cro proteins compete with prophage repressors to bind to the region controlling the prophage lysogenic/lytic switch, and they were involved in the phage infection process ( Harvey and Prell, 1981 ; Albright and Matthews, 1998 ). Here, we reasoned that CrlA may confer an antiphage protein.…”

Section: Resultsmentioning

confidence: 99%

Antitoxin CrlA of CrlTA Toxin–Antitoxin System in a Clinical Isolate Pseudomonas aeruginosa Inhibits Lytic Phage Infection

Lin

et al. 2022

Front. Microbiol.

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Pseudomonas aeruginosa is an important opportunistic pathogen in cystic fibrosis patients and immunocompromised individuals, and the toxin–antitoxin (TA) system is involved in bacterial virulence and phage resistance. However, the roles of TA systems in P. aeruginosa are relatively less studied and no phage Cro-like regulators were identified as TA components. Here, we identified and characterized a chromosome-encoded prophage Cro-like antitoxin (CrlA) in the clinical isolate P. aeruginosa WK172. CrlA neutralized the toxicity of the toxin CrlA (CrlT) which cleaves mRNA, and they formed a type II TA system. Specifically, crlA and crlT are co-transcribed and their protein products interact with each other directly. The autorepression of CrlA is abolished by CrlT through the formation of the CrlTA complex. Furthermore, crlTA is induced in the stationary phase, and crlA is expressed at higher levels than crlT. The excess CrlA inhibits the infection of lytic Pseudomonas phages. CrlA is widely distributed among Pseudomonas and in other bacterial strains and may provide antiphage activities.

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Section: Resultsmentioning

confidence: 99%

Antitoxin CrlA of CrlTA Toxin–Antitoxin System in a Clinical Isolate Pseudomonas aeruginosa Inhibits Lytic Phage Infection

Lin

et al. 2022

Front. Microbiol.

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Kinetics of c2-repressor synthesis in a regulatory defective P22 mutant

Prell¹,

Harvey²

1981

Molec. Gen. Genet.

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Phage P22 defective in gene 24 and harbouring the Oc mutation k5 in OR exhibits a strongly increased c2-repressor synthesis after infection of non-lysogenic S. typhimurium. The repressor synthesis depends strictly on an intact c1 gene. The kinetics of its synthesis, as monitored by polyacrylamide gel electrophoresis, is the same as with P22 c+, namely a turn off 8-10 min after infection. - After infection of P22-lysogenic bacteria with either P22 24- k5 or P22 24- k5 c1, much lower amounts of repressor are synthesized but again with the same kinetics. These results suggest a cro-like function acting at PRE and PRM of P22. The possible reason for the c2 overproduction is discussed.

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P22 antirepressor protein prevents in vivo recA-dependent proteolysis of P22 repressor

Prell¹,

Harvey²

1983

Mol Gen Genet

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A method was developed to demonstrate recA-dependent P22-repressor breakdown in vivo by SDS-polyacrylamide electrophoresis of unfractionated extracts of phage-infected, lysogenic Salmonella typhimurium strains TA1530 rec+ and TA1530 recA1-. The antirepressor of P22 is not cleaved by recA protein. Under conditions of unregulated ant-overproduction (Harvey et al. 1981) antirepressor protects c2-repressor in vivo against proteolytic cleavage by recA protein.

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Kinetics of P22 early gene expression suggests a cro-like regulatory function

Cited by 3 publications

References 35 publications

Antitoxin CrlA of CrlTA Toxin–Antitoxin System in a Clinical Isolate Pseudomonas aeruginosa Inhibits Lytic Phage Infection

Antitoxin CrlA of CrlTA Toxin–Antitoxin System in a Clinical Isolate Pseudomonas aeruginosa Inhibits Lytic Phage Infection

Kinetics of c2-repressor synthesis in a regulatory defective P22 mutant

P22 antirepressor protein prevents in vivo recA-dependent proteolysis of P22 repressor

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