prlF and yhaV encode a new toxin-antitoxin system in Escherichia coli.
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.
Schmidt
Oliver
O
Department of Protein Evolution, Max-Planck-Institute for Developmental Biology, 72076 Tübingen, Germany.
Schuenemann
Verena J
VJ
Department of Protein Evolution, Max-Planck-Institute for Developmental Biology, 72076 Tübingen, Germany.
Hand
Nicholas J
NJ
Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
Silhavy
Thomas J
TJ
Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
Martin
Jörg
J
Department of Protein Evolution, Max-Planck-Institute for Developmental Biology, 72076 Tübingen, Germany.
Lupas
Andrei N
AN
Department of Protein Evolution, Max-Planck-Institute for Developmental Biology, 72076 Tübingen, Germany. Electronic address: andrei.lupas@tuebingen.mpg.de.
Djuranovic
Sergej
S
Department of Protein Evolution, Max-Planck-Institute for Developmental Biology, 72076 Tübingen, Germany.
D000595:Amino Acid Sequence; D001427:Bacterial Toxins / Q000235:genetics / Q000378:metabolism* / Q000633:toxicity*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism* / Q000633:toxicity*; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes; D009876:Operon; D011401:Promoter Regions, Genetic; D012260:Ribonucleases / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D001427:Bacterial Toxins; D029968:Escherichia coli Proteins; D046912:Multiprotein Complexes; C524841:prlF protein, E coli; C524842:yhaV protein, E coli; D012260:Ribonucleases
Anal Biochem. 1970 Feb;33(2):459-63
4910776
Trends Biochem Sci. 2005 Dec;30(12):672-9
16257530
Gene. 1987;56(1):125-35
3315856
J Bacteriol. 1990 Jan;172(1):185-92
2152898
J Bacteriol. 1990 Mar;172(3):1587-94
2407727
Biotechniques. 1990 Apr;8(4):404-7
2340178
J Bacteriol. 1992 Sep;174(17):5661-8
1512198
Mol Microbiol. 2006 Aug;61(3):573-83
16803593
J Bacteriol. 2007 Sep;189(17):6101-8
17513477
Curr Biol. 1999 Oct 21;9(20):1158-68
10531028
Annu Rev Microbiol. 1999;53:43-70
10547685
Mol Microbiol. 2002 Jul;45(2):501-10
12123459
Cell. 2003 Jan 10;112(1):131-40
12526800
Mol Cell. 2003 Apr;11(4):875-84
12718874
Mol Microbiol. 2003 Jun;48(5):1389-400
12787364
J Bacteriol. 2003 Nov;185(22):6530-9
14594825
Genome Biol. 2003;4(12):R81
14659018
J Bacteriol. 1995 Jul;177(14):4121-30
7608087
J Mol Biol. 1996 Jul 19;260(3):289-98
8757792
J Bacteriol. 1996 Aug;178(15):4500-7
8755877
Nat Struct Mol Biol. 2005 Apr;12(4):327-31
15768033
Nat Rev Microbiol. 2005 May;3(5):371-82
15864262
Structure. 2005 Jun;13(6):919-28
15939023
Mol Cell. 2005 Aug 19;19(4):497-509
16109374
J Bacteriol. 1984 Jun;158(3):878-83
6233268