TY - JOUR
T1 - prlF and yhaV Encode a New Toxin-Antitoxin System in Escherichia coli
AU - Schmidt, Oliver
AU - Schuenemann, Verena J.
AU - Hand, Nicholas J.
AU - Silhavy, Thomas J.
AU - Martin, Jörg
AU - Lupas, Andrei N.
AU - Djuranovic, Sergej
N1 - Funding Information:
We thank Gerold Schwarz and Florian Altenberendt for mass spectrometry, Heinz Schwarz for electron microscopy, and Natacha Ruiz for critical reading of the manuscript. This work was supported by institutional funds from the Max Planck Society. N.J.H. and T.J.S. were supported by grant GM34821 (to T.J.S.) from the National Institute of General Medical Sciences.
PY - 2007/9/28
Y1 - 2007/9/28
N2 - 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.
AB - 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.
KW - RelE superfamily ribonuclease
KW - mRNA decay
KW - stress response
KW - swapped-hairpin barrel
KW - toxin-antitoxin system
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U2 - 10.1016/j.jmb.2007.07.016
DO - 10.1016/j.jmb.2007.07.016
M3 - Article
C2 - 17706670
AN - SCOPUS:34548445072
SN - 0022-2836
VL - 372
SP - 894
EP - 905
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 4
ER -