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          Institute: MPI für Entwicklungsbiologie     Collection: Abteilung 1 - Protein Evolution (A. Lupas)     Display Documents



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ID: 331551.0, MPI für Entwicklungsbiologie / Abteilung 1 - Protein Evolution (A. Lupas)
prlF and yhaV encode a new toxin-antitoxin system in Escherichia coli.
Authors:Schmidt, O.; Schuenemann, Verena; Hand, N.J.; Silhavy, T.J.; Martin, Joerg; Lupas, Andrei; Djuranovic, Sergej
Language:English
Date of Publication (YYYY-MM-DD):2007-09-28
Title of Journal:J Mol Biol.
Volume:372
Issue / Number:4
Start Page:894
End Page:905
Sequence Number of Article:17706670
Review Status:not specified
Audience:Not Specified
Abstract / Description:Toxin-antitoxin systems consist of a stable toxin, frequently with endonuclease activity, and a small, labile antitoxin, which sequesters the toxin into an inactive complex. Under unfavorable conditions, the antitoxin is degraded, leading to activation of the toxin and resulting in growth arrest, possibly also in bacterial programmed cell death. Correspondingly, these systems are generally viewed as agents of the stress response in prokaryotes. Here we show that prlF and yhaV encode a novel toxin-antitoxin system in Escherichia coli. YhaV, a ribonuclease of the RelE superfamily, causes reversible bacteriostasis that is counteracted by PrlF, a swapped-hairpin transcription factor homologous to MazE. The two proteins form a tight, hexameric complex, which binds with high specificity to a conserved sequence in the promoter region of the prlF-yhaV operon. As homologs of MazE and RelE, respectively, PrlF and YhaV provide an evolutionary connection between the two best-characterized toxin-antitoxin systems in E. coli, mazEF and relEB.
External Publication Status:published
Document Type:Article
Affiliations:MPI für Entwicklungsbiologie/Abteilung 1 - Proteinevolution (Andrei Lupas)
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