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Endoribonuclease toxin MazF (EC 3.1.27.-) (Toxin MazF) (mRNA interferase MazF)

 MAZF_ECOLI              Reviewed;         111 AA.
P0AE70; P33645; Q2MA50;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 1.
22-NOV-2017, entry version 94.
RecName: Full=Endoribonuclease toxin MazF;
EC=3.1.27.- {ECO:0000269|PubMed:15537630};
AltName: Full=Toxin MazF;
AltName: Full=mRNA interferase MazF {ECO:0000303|PubMed:15537630};
Name=mazF; Synonyms=chpA, chpAK; OrderedLocusNames=b2782, JW2753;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND OPERON STRUCTURE.
STRAIN=K12;
PubMed=2844820;
Metzger S., Dror I.B., Aizenman E., Schreiber G., Toone M.,
Friesen J.D., Cashel M., Glaser G.;
"The nucleotide sequence and characterization of the relA gene of
Escherichia coli.";
J. Biol. Chem. 263:15699-15704(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / MC1000 / ATCC 39531;
PubMed=8226627; DOI=10.1128/jb.175.21.6850-6856.1993;
Masuda Y., Miyakawa K., Nishimura Y., Ohtsubo E.;
"chpA and chpB, Escherichia coli chromosomal homologs of the pem locus
responsible for stable maintenance of plasmid R100.";
J. Bacteriol. 175:6850-6856(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
FUNCTION IN PROGRAMMED CELL DEATH, INTERACTION WITH MAZE, INDUCTION,
DISRUPTION PHENOTYPE, AND OPERON STRUCTURE.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=8650219; DOI=10.1073/pnas.93.12.6059;
Aizenman E., Engelberg-Kulka H., Glaser G.;
"An Escherichia coli chromosomal 'addiction module' regulated by
guanosine 3',5'-bispyrophosphate: a model for programmed bacterial
cell death.";
Proc. Natl. Acad. Sci. U.S.A. 93:6059-6063(1996).
[6]
TRANSCRIPTION REGULATION, AND SUBUNIT.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=11071896; DOI=10.1074/jbc.M008832200;
Marianovsky I., Aizenman E., Engelberg-Kulka H., Glaser G.;
"The regulation of the Escherichia coli mazEF promoter involves an
unusual alternating palindrome.";
J. Biol. Chem. 276:5975-5984(2001).
[7]
FUNCTION IN CELL DEATH, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=11222603; DOI=10.1128/JB.183.6.2041-2045.2001;
Sat B., Hazan R., Fisher T., Khaner H., Glaser G., Engelberg-Kulka H.;
"Programmed cell death in Escherichia coli: some antibiotics can
trigger mazEF lethality.";
J. Bacteriol. 183:2041-2045(2001).
[8]
FUNCTION AS A TOXIN.
STRAIN=K12;
PubMed=12123459; DOI=10.1046/j.1365-2958.2002.03027.x;
Pedersen K., Christensen S.K., Gerdes K.;
"Rapid induction and reversal of a bacteriostatic condition by
controlled expression of toxins and antitoxins.";
Mol. Microbiol. 45:501-510(2002).
[9]
RNA CLEAVAGE, INDUCTION, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=12972253; DOI=10.1016/S0022-2836(03)00922-7;
Christensen S.K., Pedersen K., Hansen F.G., Gerdes K.;
"Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and
ChpBK cleave translated RNAs and are counteracted by tmRNA.";
J. Mol. Biol. 332:809-819(2003).
[10]
DISRUPTION PHENOTYPE, FUNCTION IN STRESS RESPONSE, AND DEPENDENCE ON
RELA.
STRAIN=K12 / K38 / S26, and K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=15150257; DOI=10.1128/JB.186.11.3663-3669.2004;
Hazan R., Sat B., Engelberg-Kulka H.;
"Escherichia coli mazEF-mediated cell death is triggered by various
stressful conditions.";
J. Bacteriol. 186:3663-3669(2004).
[11]
FUNCTION IN PROGRAMMED CELL DEATH.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=15576778; DOI=10.1128/JB.186.24.8295-8300.2004;
Amitai S., Yassin Y., Engelberg-Kulka H.;
"MazF-mediated cell death in Escherichia coli: a point of no return.";
J. Bacteriol. 186:8295-8300(2004).
[12]
FUNCTION IN PHAGE IMMUNITY, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / JM109 / ATCC 53323, K12 / K38 / S26, and
K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=15316771; DOI=10.1007/s00438-004-1048-y;
Hazan R., Engelberg-Kulka H.;
"Escherichia coli mazEF-mediated cell death as a defense mechanism
that inhibits the spread of phage P1.";
Mol. Genet. Genomics 272:227-234(2004).
[13]
FUNCTION AS AN ENDONUCLEASE, ENZYME REGULATION, SUBSTRATE SPECIFICITY,
AND RNA-BINDING.
PubMed=15537630; DOI=10.1074/jbc.M411811200;
Zhang Y., Zhang J., Hara H., Kato I., Inouye M.;
"Insights into the mRNA cleavage mechanism by MazF, an mRNA
interferase.";
J. Biol. Chem. 280:3143-3150(2005).
[14]
BIOTECHNOLOGY.
PubMed=15837428; DOI=10.1016/j.molcel.2005.03.011;
Suzuki M., Zhang J., Liu M., Woychik N.A., Inouye M.;
"Single protein production in living cells facilitated by an mRNA
interferase.";
Mol. Cell 18:253-261(2005).
[15]
INDUCTION, AND OPERON STRUCTURE.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574, and
K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16390452; DOI=10.1111/j.1365-2958.2005.04956.x;
Gross M., Marianovsky I., Glaser G.;
"MazG -- a regulator of programmed cell death in Escherichia coli.";
Mol. Microbiol. 59:590-601(2006).
[16]
REQUIREMENT FOR EXTRACELLULAR DEATH FACTOR (EDF).
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=17962566; DOI=10.1126/science.1147248;
Kolodkin-Gal I., Hazan R., Gaathon A., Carmeli S., Engelberg-Kulka H.;
"A linear pentapeptide is a quorum-sensing factor required for mazEF-
mediated cell death in Escherichia coli.";
Science 318:652-655(2007).
[17]
EDF PRODUCTION, AND STRAIN DIFFERENCES IN ABILITY TO MAKE AND RESPOND
TO EDF.
STRAIN=K12 / K38 / S26, K12 / MC4100 / ATCC 35695 / DSM 6574,
K12 / MG1655 / ATCC 47076, and K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=18310334; DOI=10.1128/JB.01918-07;
Kolodkin-Gal I., Engelberg-Kulka H.;
"The extracellular death factor: physiological and genetic factors
influencing its production and response in Escherichia coli.";
J. Bacteriol. 190:3169-3175(2008).
[18]
TRANSLATION IMPROVES CLEAVAGE EFFICIENCY.
STRAIN=K12;
PubMed=18854355; DOI=10.1093/nar/gkn667;
Christensen-Dalsgaard M., Gerdes K.;
"Translation affects YoeB and MazF messenger RNA interferase
activities by different mechanisms.";
Nucleic Acids Res. 36:6472-6481(2008).
[19]
FUNCTION.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=19251848; DOI=10.1128/JB.00011-09;
Kolodkin-Gal I., Engelberg-Kulka H.;
"The stationary-phase sigma factor sigma(S) is responsible for the
resistance of Escherichia coli stationary-phase cells to mazEF-
mediated cell death.";
J. Bacteriol. 191:3177-3182(2009).
[20]
FUNCTION IN CELL DEATH, FUNCTION IN BIOFILM FORMATION, AND DISRUPTION
PHENOTYPE.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=19707553; DOI=10.1371/journal.pone.0006785;
Kolodkin-Gal I., Verdiger R., Shlosberg-Fedida A., Engelberg-Kulka H.;
"A differential effect of E. coli toxin-antitoxin systems on cell
death in liquid media and biofilm formation.";
PLoS ONE 4:E6785-E6785(2009).
[21]
FUNCTION, SUBSTRATE SPECIFICITY, AND TRANSLATION REGULATION.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=21944167; DOI=10.1016/j.cell.2011.07.047;
Vesper O., Amitai S., Belitsky M., Byrgazov K., Kaberdina A.C.,
Engelberg-Kulka H., Moll I.;
"Selective translation of leaderless mRNAs by specialized ribosomes
generated by MazF in Escherichia coli.";
Cell 147:147-157(2011).
[22]
FUNCTION, ENZYME REGULATION, INTERACTION WITH EDF, AND SUBUNIT.
PubMed=21419338; DOI=10.1016/j.molcel.2011.02.023;
Belitsky M., Avshalom H., Erental A., Yelin I., Kumar S., London N.,
Sperber M., Schueler-Furman O., Engelberg-Kulka H.;
"The Escherichia coli extracellular death factor EDF induces the
endoribonucleolytic activities of the toxins MazF and ChpBK.";
Mol. Cell 41:625-635(2011).
[23]
FUNCTION IN PERSISTENCE, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=21788497; DOI=10.1073/pnas.1100186108;
Maisonneuve E., Shakespeare L.J., Joergensen M.G., Gerdes K.;
"Bacterial persistence by RNA endonucleases.";
Proc. Natl. Acad. Sci. U.S.A. 108:13206-13211(2011).
[24]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
Walker G.C.;
"Hydroxyurea induces hydroxyl radical-mediated cell death in
Escherichia coli.";
Mol. Cell 36:845-860(2009).
[25]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=22412352; DOI=10.1371/journal.pbio.1001281;
Erental A., Sharon I., Engelberg-Kulka H.;
"Two programmed cell death systems in Escherichia coli: an apoptotic-
like death is inhibited by the mazEF-mediated death pathway.";
PLoS Biol. 10:E1001281-E1001281(2012).
[26]
FUNCTION, AND INDUCTION BY OTHER TA SYSTEMS.
STRAIN=K12 / BW25113;
PubMed=23432955; DOI=10.1186/1471-2180-13-45;
Kasari V., Mets T., Tenson T., Kaldalu N.;
"Transcriptional cross-activation between toxin-antitoxin systems of
Escherichia coli.";
BMC Microbiol. 13:45-45(2013).
[27]
FUNCTION, ENZYME REGULATION, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=23416055; DOI=10.1016/j.celrep.2013.01.026;
Dorsey-Oresto A., Lu T., Mosel M., Wang X., Salz T., Drlica K.,
Zhao X.;
"YihE kinase is a central regulator of programmed cell death in
bacteria.";
Cell Rep. 3:528-537(2013).
[28]
FUNCTION, SUBSTRATE SPECIFICITY, DOMAIN, AND MUTAGENESIS OF
17-PHE--HIS-28 AND 53-THR--GLU-61.
STRAIN=K12 / BW25113;
PubMed=23280569; DOI=10.1002/prot.24246;
Park J.H., Yoshizumi S., Yamaguchi Y., Wu K.P., Inouye M.;
"ACA-specific RNA sequence recognition is acquired via the loop 2
region of MazF mRNA interferase.";
Proteins 81:874-883(2013).
[29]
FUNCTION IN PERSISTENCE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
GLU-24 AND HIS-28.
STRAIN=K12 / BW25113, and K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=24375411; DOI=10.1074/jbc.M113.510511;
Tripathi A., Dewan P.C., Siddique S.A., Varadarajan R.;
"MazF-induced growth inhibition and persister generation in
Escherichia coli.";
J. Biol. Chem. 289:4191-4205(2014).
[30]
FUNCTION IN TRANSCRIPTION, AND SUBUNIT.
PubMed=25564525; DOI=10.1093/nar/gku1352;
Zorzini V., Buts L., Schrank E., Sterckx Y.G., Respondek M.,
Engelberg-Kulka H., Loris R., Zangger K., van Nuland N.A.;
"Escherichia coli antitoxin MazE as transcription factor: insights
into MazE-DNA binding.";
Nucleic Acids Res. 43:1241-1256(2015).
[31]
REVIEW.
PubMed=19215780; DOI=10.1016/S0079-6603(08)00812-X;
Yamaguchi Y., Inouye M.;
"mRNA interferases, sequence-specific endoribonucleases from the
toxin-antitoxin systems.";
Prog. Mol. Biol. Transl. Sci. 85:467-500(2009).
[32]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-111, POSSIBLE DNA-BINDING,
AND SUBUNIT.
PubMed=12718874; DOI=10.1016/S1097-2765(03)00097-2;
Kamada K., Hanaoka F., Burley S.K.;
"Crystal structure of the MazE/MazF complex: molecular bases of
antidote-toxin recognition.";
Mol. Cell 11:875-884(2003).
[33]
STRUCTURE BY NMR, AND MUTAGENESIS OF GLU-24.
PubMed=16413577; DOI=10.1016/j.jmb.2005.12.035;
Li G.Y., Zhang Y., Chan M.C., Mal T.K., Hoeflich K.P., Inouye M.,
Ikura M.;
"Characterization of dual substrate binding sites in the homodimeric
structure of Escherichia coli mRNA interferase MazF.";
J. Mol. Biol. 357:139-150(2006).
[34]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
Wang X., Wang K., Gao X., Zhang X., Li L., Su X., Zhang J.;
"Biochemical and structural analysis of E. coli MazF toxin.";
Submitted (JUN-2010) to the PDB data bank.
-!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA)
module. A sequence-specific endoribonuclease it inhibits protein
synthesis by cleaving mRNA and inducing bacterial stasis. It is
stable, single-strand specific with mRNA cleavage independent of
the ribosome, although translation enhances cleavage for some
mRNAs (PubMed:18854355). Cleavage occurs at the 5'-end of ACA
sequences, yielding a 2',3'-cyclic phosphate and a free 5'-OH,
although cleavage can also occur on the 3'-end of the first A
(PubMed:15537630, PubMed:23280569). Digests 16S rRNA in vivo 43
nts upstream of the C-terminus; this removes the anti-Shine-
Dalgarno sequence forming a mixed population of wild-type and
"stress ribosomes". Stress ribosomes do not translate leader-
containing mRNA but are proficient in translation of leaderless
mRNA, which alters the protein expression profile of the cell;
MazF produces some leaderless mRNA (PubMed:21944167). The toxic
endoribonuclease activity is inhibited by its labile cognate
antitoxin MazE. Toxicity results when the levels of MazE decrease
in the cell, leading to mRNA degradation. This effect can be
rescued by expression of MazE, but after 6 hours in rich medium
overexpression of MazF leads to programmed cell death
(PubMed:8650219, PubMed:11222603). MazF-mediated cell death occurs
following a number of stress conditions in a relA-dependent
fashion and only when cells are in log phase; sigma factor S
(rpoS) protects stationary phase cells from MazF-killing
(PubMed:15150257, PubMed:19251848). Cell growth and viability are
not affected when MazF and MazE are coexpressed. Both MazE and
MazE-MazF bind to the promoter region of the mazE-mazF operon to
inhibit their own transcription. MazE has higher affinity for
promoter DNA in the presence of MazF (PubMed:25564525). Cross-talk
can occur between different TA modules, ectopic expression of this
toxin induces transcription of the relBEF TA module operon with
specific cleavage of the mRNA produced (PubMed:23432955).
{ECO:0000269|PubMed:11071896, ECO:0000269|PubMed:11222603,
ECO:0000269|PubMed:15150257, ECO:0000269|PubMed:15537630,
ECO:0000269|PubMed:18854355, ECO:0000269|PubMed:19251848,
ECO:0000269|PubMed:21944167, ECO:0000269|PubMed:23280569,
ECO:0000269|PubMed:23432955, ECO:0000269|PubMed:25564525,
ECO:0000269|PubMed:8650219}.
-!- FUNCTION: Might also serve to protect cells against bacteriophage;
in the presence of MazE-MazF fewer P1 phage are produced than in a
disrupted strain. For strain K38 most wild-type cells are killed
but not by phage lysis; it was suggested that MazE-MazF causes P1
phage exclusion from the bacterial population. This phenomenon is
strain dependent. {ECO:0000269|PubMed:15316771}.
-!- FUNCTION: The physiological role of this TA module is debated.
Programmed cell death (PCD) occurs when cells are at high density
and depends on the presence of MazE-MazF and a quorum sensing
pentapeptide, the extracellular death factor (EDF) with sequence
Asn-Asn-Trp-Asn-Asn (NNWNN), probably produced from the zwf gene
product glucose-6-phosphate 1-dehydrogenase (PubMed:17962566,
PubMed:18310334). Cell death governed by the MazE-MazF and DinJ-
YafQ TA modules seems to play a role in biofilm formation, while
MazE-MazF is also implicated in cell death in liquid media
(PubMed:19707553). Implicated in hydroxy radical-mediated cell
death induced by hydroxyurea treatment (PubMed:20005847,
PubMed:23416055). In conjunction with EDF prevents apoptotic-like
death (ALD) in the presence of DNA damaging agents, probably by
reducing recA mRNA levels in a non-endonuclease-mediated manner
(PubMed:22412352). Other studies (in strains BW25113 and MC4100,
the latter makes EDF) demonstrate MazF does not cause PCD but
instead bacteriostasis and possibly a dormant state as well as
persister cell generation (PubMed:24375411). mRNA interferases
play a role in bacterial persistence to antibiotics;
overexpression of this protein induces persisters resistant to
ciprofloxacin and ampicillin (PubMed:21788497).
{ECO:0000269|PubMed:17962566, ECO:0000269|PubMed:18310334,
ECO:0000269|PubMed:19707553, ECO:0000269|PubMed:20005847,
ECO:0000269|PubMed:21419338, ECO:0000269|PubMed:21788497,
ECO:0000269|PubMed:22412352, ECO:0000269|PubMed:23416055,
ECO:0000269|PubMed:24375411, ECO:0000269|PubMed:8650219}.
-!- ENZYME REGULATION: Inhibited by Mg(2+) (PubMed:15537630).
Stimulated in vitro in a concentration-dependent fashion by EDF,
which is able to overcome inhibition by cognate antitoxin MazE
(PubMed:21419338). The TA module is antagonized by stress response
kinase SrkA, but probably not by phosphorylation of MazF
(PubMed:23416055). {ECO:0000269|PubMed:15537630,
ECO:0000269|PubMed:21419338, ECO:0000269|PubMed:23416055}.
-!- SUBUNIT: Probably a dimer. Forms a heterohexamer composed of
alternating toxin and antitoxin homodimers MazF(2)-MazE(2)-
MazF(2). The binding site of MazE and ssRNA or ssDNA are largely
overlapping; the presence of only 1 MazE molecule inhibits mRNA
endoribonuclease activity. Binds to EDF but not a mutated EDF
(NNGNN) (PubMed:21419338). {ECO:0000269|PubMed:11071896,
ECO:0000269|PubMed:12718874, ECO:0000269|PubMed:21419338,
ECO:0000269|PubMed:25564525, ECO:0000269|PubMed:8650219}.
-!- INDUCTION: Expressed in exponentially growing cells. Induction has
been reported to occur after amino acid starvation in a ppGpp-
independent fashion and to be Lon protease-dependent
(PubMed:12972253), but also to not occur after amino acid
starvation and to be regulated by ppGpp (PubMed:8650219). Also
induced in M9 minimal medium and by chloramphenicol treatment
(PubMed:21944167). MazE alone and in combination with MazF,
represses transcription of the mazE-mazF operon. Fis activates
transcription. Part of the relA-mazE-mazF-mazG operon, there is
also a second mazE-mazF specific promoter which is negatively
autoregulated (PubMed:2844820, PubMed:8650219). Operon induced by
ectopic expression of toxin RelE; operon induction by amino acid
starvation requires the relBEF operon (PubMed:23432955).
{ECO:0000269|PubMed:11071896, ECO:0000269|PubMed:12972253,
ECO:0000269|PubMed:16390452, ECO:0000269|PubMed:21944167,
ECO:0000269|PubMed:23432955, ECO:0000269|PubMed:2844820,
ECO:0000269|PubMed:8650219}.
-!- DOMAIN: Loop 1 (residues 17-28) effects catalytic activity while
recognition of the ACA cleavage site is influenced by loop 2
(residues 53-61). Alterations of loop 2 generate new cleavage
sites in addition to retaining the original cleavage site.
{ECO:0000305|PubMed:23280569}.
-!- DISRUPTION PHENOTYPE: Decreased sensitivity to dramatic
intracellular increases of ppGpp. Cells missing mazE-mazF survive
high temperature, various DNA-damaging agents and H(2)O(2)
exposure better than wild-type cells. Cells missing mazE-mazF
produce more P1 phage than wild-type cells, while introduction of
lysogens into a growing non-lysogenic disruption culture is lethal
(PubMed:15316771). Cells missing mazE-mazF show reduced biofilm
formation, and survive antibiotic treatment in log phase better
than wild-type cells (PubMed:11222603, PubMed:19707553). However
lag phase cells disrupted only for mazF had a lower survival rate
than wild-type cells (PubMed:24375411). Cells missing mazE-mazF
survive hydroxyurea treatment better than wild-type; further
disruption of relE-relB and tonB yields even better survival
(PubMed:20005847). Cells missing mazE-mazF undergo an apoptotic-
like death (ALD) upon DNA damage characterized by membrane
depolarization and DNA fragmentation; further disruption of recA
prevents membrane depolarization (PubMed:22412352). Unlike the
single srkA disruption mutant, a triple srkA-mazE-mazF disruption
mutant shows no hyperlethality in the presence of nalidixic acid
or UV light, suggesting SrkA has a negative effect on MazF
(PubMed:23416055). mRNA interferases play a role in bacterial
persistence to antibiotics; as 10 mRNA interferases are
successively deleted reduced levels of persisters are generated
(PubMed:21788497). {ECO:0000269|PubMed:11222603,
ECO:0000269|PubMed:12972253, ECO:0000269|PubMed:15150257,
ECO:0000269|PubMed:15316771, ECO:0000269|PubMed:19707553,
ECO:0000269|PubMed:20005847, ECO:0000269|PubMed:21788497,
ECO:0000269|PubMed:22412352, ECO:0000269|PubMed:23416055,
ECO:0000269|PubMed:24375411, ECO:0000269|PubMed:8650219}.
-!- BIOTECHNOLOGY: Can be used to produce large quantities of a single
protein if the gene coding for the protein does not contain any
ACA codons. Up to 90% of expressed bacterial cellular protein can
be the target, which can be produced for up to 4 days. The system
also works in eukaryotic cells. {ECO:0000269|PubMed:15837428}.
-!- SIMILARITY: Belongs to the PemK/MazF family. {ECO:0000305}.
-!- CAUTION: Strain K12 / MG1655 is deficient in both production and
response to EDF, unlike strains K12 / MC4100, K12 / W3110 and K12
/ K38, all of which make and respond to EDF.
{ECO:0000269|PubMed:18310334}.
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EMBL; D16450; BAA03918.1; -; Genomic_DNA.
EMBL; J04039; AAA03239.1; -; Unassigned_DNA.
EMBL; U29580; AAA69292.1; -; Genomic_DNA.
EMBL; U00096; AAC75824.1; -; Genomic_DNA.
EMBL; AP009048; BAE76856.1; -; Genomic_DNA.
PIR; B49339; B49339.
RefSeq; NP_417262.1; NC_000913.3.
RefSeq; WP_000254738.1; NZ_LN832404.1.
PDB; 1UB4; X-ray; 1.70 A; A/B=2-111.
PDB; 3NFC; X-ray; 2.00 A; A/B/C/D/E/F=1-111.
PDB; 5CK9; X-ray; 1.90 A; A/B=1-111.
PDB; 5CKB; X-ray; 2.80 A; A/B=1-111.
PDB; 5CKD; X-ray; 1.70 A; A/B=1-111.
PDB; 5CKE; X-ray; 2.31 A; A/B=1-111.
PDB; 5CKF; X-ray; 2.80 A; A/B=1-111.
PDB; 5CKH; X-ray; 2.45 A; A/B=1-111.
PDB; 5CO7; X-ray; 3.49 A; A/B/C/D/E/F=1-111.
PDB; 5CQX; X-ray; 1.63 A; A/B=1-111.
PDB; 5CQY; X-ray; 2.48 A; A/B=1-111.
PDB; 5CR2; X-ray; 2.90 A; A/B/C=1-111.
PDBsum; 1UB4; -.
PDBsum; 3NFC; -.
PDBsum; 5CK9; -.
PDBsum; 5CKB; -.
PDBsum; 5CKD; -.
PDBsum; 5CKE; -.
PDBsum; 5CKF; -.
PDBsum; 5CKH; -.
PDBsum; 5CO7; -.
PDBsum; 5CQX; -.
PDBsum; 5CQY; -.
PDBsum; 5CR2; -.
DisProt; DP00299; -.
ProteinModelPortal; P0AE70; -.
SMR; P0AE70; -.
BioGrid; 4262300; 13.
IntAct; P0AE70; 2.
STRING; 316385.ECDH10B_2949; -.
BindingDB; P0AE70; -.
ChEMBL; CHEMBL1795096; -.
PaxDb; P0AE70; -.
PRIDE; P0AE70; -.
EnsemblBacteria; AAC75824; AAC75824; b2782.
EnsemblBacteria; BAE76856; BAE76856; BAE76856.
GeneID; 947252; -.
KEGG; ecj:JW2753; -.
KEGG; eco:b2782; -.
PATRIC; fig|1411691.4.peg.3953; -.
EchoBASE; EB1229; -.
EcoGene; EG11249; mazF.
eggNOG; ENOG4105MZG; Bacteria.
eggNOG; COG2337; LUCA.
HOGENOM; HOG000290185; -.
InParanoid; P0AE70; -.
KO; K07171; -.
PhylomeDB; P0AE70; -.
BioCyc; EcoCyc:EG11249-MONOMER; -.
BioCyc; MetaCyc:EG11249-MONOMER; -.
EvolutionaryTrace; P0AE70; -.
PRO; PR:P0AE70; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0043234; C:protein complex; IDA:CAFA.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0004521; F:endoribonuclease activity; IDA:UniProtKB.
GO; GO:0032403; F:protein complex binding; IDA:CAFA.
GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0006402; P:mRNA catabolic process; IDA:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
GO; GO:0051291; P:protein heterooligomerization; IDA:CAFA.
GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
GO; GO:0016075; P:rRNA catabolic process; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 2.30.30.110; -; 1.
InterPro; IPR003477; PemK-like.
InterPro; IPR011067; Plasmid_toxin/cell-grow_inhib.
Pfam; PF02452; PemK_toxin; 1.
SUPFAM; SSF50118; SSF50118; 1.
1: Evidence at protein level;
3D-structure; Antiviral defense; Complete proteome; DNA-binding;
Endonuclease; Hydrolase; Nuclease; Quorum sensing; Reference proteome;
Repressor; RNA-binding; Stress response; Transcription;
Transcription regulation; Translation regulation.
CHAIN 1 111 Endoribonuclease toxin MazF.
/FTId=PRO_0000201897.
REGION 17 28 Loop 1, participates in catalytic
activity. {ECO:0000305|PubMed:23280569}.
REGION 53 61 Loop 2, involved in substrate
recognition.
{ECO:0000305|PubMed:23280569}.
MUTAGEN 17 28 FDPTKGSEQAGH->GGGGGGGGGGG: Changes loop 1
to poly-G; loss of endoribonuclease
activity. {ECO:0000269|PubMed:23280569}.
MUTAGEN 17 28 FDPTKGSEQAGH->LGPPSGSQPAKR: Changes loop
1 to MazF6 M.tuberculosis sequence; loss
of endoribonuclease activity.
{ECO:0000269|PubMed:23280569}.
MUTAGEN 17 28 FDPTKGSEQAGH->PDDSRGPVPSYS: Changes loop
1 to MazF M.xanthus sequence; loss of
endoribonuclease activity.
{ECO:0000269|PubMed:23280569}.
MUTAGEN 24 24 E->A: Greatly reduces toxicity, about 10-
fold less RNA cleavage activity.
Expression in the presence of wt MazF has
a dominant-negative phenotype, causing
cell death as it titrates out the MazE
antitoxin; still activates operon
transcription.
{ECO:0000269|PubMed:16413577,
ECO:0000269|PubMed:24375411}.
MUTAGEN 28 28 H->A: No changes in toxicity.
{ECO:0000269|PubMed:24375411}.
MUTAGEN 53 61 TQSKGYPFE->GGGGGGGG,GGGGGGGGGGG: Changes
loop 2 to poly-G; reduces
endoribonuclease activity, alters
cleavage sites.
{ECO:0000269|PubMed:23280569}.
MUTAGEN 53 61 TQSKGYPFE->SNLHRASEPGN: Changes loop 2 to
MazF M.xanthus sequence; reduces
endoribonuclease activity, alters
cleavage sites.
{ECO:0000269|PubMed:23280569}.
MUTAGEN 53 61 TQSKGYPFE->SNTALAAMPGN: Changes loop 2 to
MazF6 M.tuberculosis sequence; reduces
endoribonuclease activity, alters
cleavage sites.
{ECO:0000269|PubMed:23280569}.
STRAND 11 15 {ECO:0000244|PDB:5CQX}.
TURN 19 22 {ECO:0000244|PDB:5CQX}.
STRAND 29 33 {ECO:0000244|PDB:5CQX}.
HELIX 37 43 {ECO:0000244|PDB:5CQX}.
STRAND 46 53 {ECO:0000244|PDB:5CQX}.
STRAND 61 63 {ECO:0000244|PDB:5CQX}.
STRAND 66 69 {ECO:0000244|PDB:5CKD}.
STRAND 72 74 {ECO:0000244|PDB:5CQX}.
HELIX 75 77 {ECO:0000244|PDB:5CQX}.
STRAND 79 81 {ECO:0000244|PDB:5CQX}.
HELIX 83 86 {ECO:0000244|PDB:5CQX}.
STRAND 89 93 {ECO:0000244|PDB:5CQX}.
HELIX 96 110 {ECO:0000244|PDB:5CQX}.
SEQUENCE 111 AA; 12098 MW; 1579C867DD6B96AC CRC64;
MVSRYVPDMG DLIWVDFDPT KGSEQAGHRP AVVLSPFMYN NKTGMCLCVP CTTQSKGYPF
EVVLSGQERD GVALADQVKS IAWRARGATK KGTVAPEELQ LIKAKINVLI G


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