MQSR_ECOLI
ID MQSR_ECOLI Reviewed; 98 AA.
AC Q46865; Q2M9H8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=mRNA interferase toxin MqsR {ECO:0000303|PubMed:19690171};
DE EC=3.1.-.-;
DE AltName: Full=Endoribonuclease MqsR;
DE AltName: Full=Motility quorum-sensing regulator MqsR {ECO:0000303|PubMed:16352847};
DE AltName: Full=Toxin MqsR;
GN Name=mqsR {ECO:0000303|PubMed:16352847}; Synonyms=ygiU;
GN OrderedLocusNames=b3022, JW2990;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP IDENTIFICATION AS A TOXIN-ANTITOXIN SYSTEM, INDUCTION IN PERSISTER CELLS,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=16768798; DOI=10.1186/1471-2180-6-53;
RA Shah D., Zhang Z., Khodursky A., Kaldalu N., Kurg K., Lewis K.;
RT "Persisters: a distinct physiological state of E. coli.";
RL BMC Microbiol. 6:53-53(2006).
RN [4]
RP FUNCTION AS A REGULATOR OF BIOFILM FORMATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / ATCC 25404 / DSM 5698 / NCIMB 11290, K12 / DH5-alpha, and
RC K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16352847; DOI=10.1128/jb.188.1.305-316.2006;
RA Gonzalez Barrios A.F., Zuo R., Hashimoto Y., Yang L., Bentley W.E.,
RA Wood T.K.;
RT "Autoinducer 2 controls biofilm formation in Escherichia coli through a
RT novel motility quorum-sensing regulator (MqsR, B3022).";
RL J. Bacteriol. 188:305-316(2006).
RN [5]
RP FUNCTION AS AN MRNA INTERFERASE, FUNCTION AS A TRANSCRIPTIONAL REGULATOR,
RP SUBUNIT, ACTIVITY REGULATION, AND OPERON STRUCTURE.
RX PubMed=19690171; DOI=10.1074/jbc.m109.032904;
RA Yamaguchi Y., Park J.H., Inouye M.;
RT "MqsR, a crucial regulator for quorum sensing and biofilm formation, is a
RT GCU-specific mRNA interferase in Escherichia coli.";
RL J. Biol. Chem. 284:28746-28753(2009).
RN [6]
RP FUNCTION IN PERSISTER CELL FORMATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=19909729; DOI=10.1016/j.bbrc.2009.11.033;
RA Kim Y., Wood T.K.;
RT "Toxins Hha and CspD and small RNA regulator Hfq are involved in persister
RT cell formation through MqsR in Escherichia coli.";
RL Biochem. Biophys. Res. Commun. 391:209-213(2010).
RN [7]
RP FUNCTION AS AN MRNA INTERFERASE, FUNCTION AS A TRANSCRIPTION REGULATOR,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113, and K12 / MG1655 / ATCC 47076;
RX PubMed=20105222; DOI=10.1111/j.1462-2920.2009.02147.x;
RA Kim Y., Wang X., Zhang X.S., Grigoriu S., Page R., Peti W., Wood T.K.;
RT "Escherichia coli toxin/antitoxin pair MqsR/MqsA regulate toxin CspD.";
RL Environ. Microbiol. 12:1105-1121(2010).
RN [8]
RP FUNCTION AS AN MRNA INTERFERASE, INDUCTION, AND OPERON STRUCTURE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19943910; DOI=10.1111/j.1365-2958.2009.06969.x;
RA Christensen-Dalsgaard M., Jorgensen M.G., Gerdes K.;
RT "Three new RelE-homologous mRNA interferases of Escherichia coli
RT differentially induced by environmental stresses.";
RL Mol. Microbiol. 75:333-348(2010).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21516113; DOI=10.1038/nchembio.560;
RA Wang X., Kim Y., Hong S.H., Ma Q., Brown B.L., Pu M., Tarone A.M.,
RA Benedik M.J., Peti W., Page R., Wood T.K.;
RT "Antitoxin MqsA helps mediate the bacterial general stress response.";
RL Nat. Chem. Biol. 7:359-366(2011).
RN [10]
RP RETRACTED PAPER.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21788497; DOI=10.1073/pnas.1100186108;
RA Maisonneuve E., Shakespeare L.J., Joergensen M.G., Gerdes K.;
RT "Bacterial persistence by RNA endonucleases.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13206-13211(2011).
RN [11]
RP RETRACTION NOTICE OF PUBMED:21788497.
RX PubMed=29531044; DOI=10.1073/pnas.1803278115;
RA Maisonneuve E., Shakespeare L.J., Joergensen M.G., Gerdes K.;
RL Proc. Natl. Acad. Sci. U.S.A. 115:E2901-E2901(2018).
RN [12]
RP FUNCTION, AND INDUCTION BY OTHER TA SYSTEMS.
RC STRAIN=K12 / BW25113;
RX PubMed=23432955; DOI=10.1186/1471-2180-13-45;
RA Kasari V., Mets T., Tenson T., Kaldalu N.;
RT "Transcriptional cross-activation between toxin-antitoxin systems of
RT Escherichia coli.";
RL BMC Microbiol. 13:45-45(2013).
RN [13]
RP FUNCTION, AND INDUCTION.
RC STRAIN=K12 / BW25113;
RX PubMed=23289863; DOI=10.1111/1462-2920.12063;
RA Wang X., Lord D.M., Hong S.H., Peti W., Benedik M.J., Page R., Wood T.K.;
RT "Type II toxin/antitoxin MqsR/MqsA controls type V toxin/antitoxin
RT GhoT/GhoS.";
RL Environ. Microbiol. 15:1734-1744(2013).
RN [14]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND LACK OF
RP DNA-BINDING.
RX PubMed=23172222; DOI=10.1074/jbc.m112.421008;
RA Brown B.L., Lord D.M., Grigoriu S., Peti W., Page R.;
RT "The Escherichia coli toxin MqsR destabilizes the transcriptional
RT repression complex formed between the antitoxin MqsA and the mqsRA operon
RT promoter.";
RL J. Biol. Chem. 288:1286-1294(2013).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=25534751; DOI=10.1111/1462-2920.12749;
RA Kwan B.W., Lord D.M., Peti W., Page R., Benedik M.J., Wood T.K.;
RT "The MqsR/MqsA toxin/antitoxin system protects Escherichia coli during bile
RT acid stress.";
RL Environ. Microbiol. 17:3168-3181(2015).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH MQSA, FUNCTION AS AN
RP MRNA INTERFERASE, SUBUNIT, AND MUTAGENESIS OF TYR-55; LYS-56; MET-58;
RP GLN-68; ARG-72; TYR-81 AND LYS-96.
RC STRAIN=K12;
RX PubMed=20041169; DOI=10.1371/journal.ppat.1000706;
RA Brown B.L., Grigoriu S., Kim Y., Arruda J.M., Davenport A., Wood T.K.,
RA Peti W., Page R.;
RT "Three dimensional structure of the MqsR:MqsA complex: a novel TA pair
RT comprised of a toxin homologous to RelE and an antitoxin with unique
RT properties.";
RL PLoS Pathog. 5:E1000706-E1000706(2009).
CC -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system.
CC Plays a significant role in the control of biofilm formation and
CC induction of persister cells in the presence of antibiotics. An mRNA
CC interferase which has been reported to be translation-independent
CC (PubMed:19690171, PubMed:19943910, PubMed:23289863). It has also been
CC reported to be translation-dependent (PubMed:20041169). Cleavage has
CC been reported to occur on either side of G in the sequence GCU
CC (PubMed:19690171). Also reported to cleave after C in GC(A/U) sequences
CC (PubMed:19943910). There are only 14 genes in E.coli W3110 (and
CC probably also MG1655) that do not have a GCU sequence and thus are
CC resistant to the mRNA interferase activity; among these is the gene for
CC toxin GhoT. Overexpression of MqsR causes cessation of cell growth and
CC inhibits cell proliferation via inhibition of translation as well as
CC increasing persister cell formation; these effects are overcome by
CC concomitant or subsequent expression of antitoxin MqsA. Cross-talk can
CC occur between different TA systems. Ectopic expression of this toxin
CC induces transcription of the relBEF TA system operon with specific
CC cleavage of the relBEF mRNA produced (PubMed:23432955). Regulates the
CC expression of GhoT/GhoS, a type V TA system (PubMed:23289863).
CC Persistence depends on toxin GhoT activity, which MqsR controls at the
CC post-transcriptional level by selectively degrading the antitoxin ghoS
CC segment of the ghoST mRNA (PubMed:23289863). Overexpression leads to a
CC dramatic increase in tolerance to the antibiotic ofloxacin. This TA
CC system mediates cell growth during bile acid deoxycholate stress by
CC degrading mRNA for probable deoxycholate-binding protein YgiS; bile
CC acid detergents such as deoxycholate are important for host defense
CC against bacterial growth in the gall bladder and duodenum
CC (PubMed:25534751). {ECO:0000269|PubMed:19690171,
CC ECO:0000269|PubMed:19943910, ECO:0000269|PubMed:20041169,
CC ECO:0000269|PubMed:23289863, ECO:0000269|PubMed:23432955,
CC ECO:0000269|PubMed:25534751}.
CC -!- FUNCTION: Initially reported to act as a cotranscription factor with
CC MqsA (PubMed:19690171, PubMed:20105222). Following further experiments,
CC the MqsR-MqsA complex does not bind DNA and all reported data are
CC actually due to a small fraction of free MqsA alone binding DNA.
CC Addition of MqsR to a preformed MqsA-promoter DNA complex causes
CC dissociation of the MqsA-DNA complex, probably causing derepression of
CC MqsA-repressed transcripts. Does not bind DNA in the presence or
CC absence of MqsA (PubMed:23172222). {ECO:0000269|PubMed:19690171,
CC ECO:0000269|PubMed:20105222, ECO:0000269|PubMed:23172222}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC The MqsR-MqsA complex is exceptionally thermostable with a Tm of 83.4
CC degress Celsius versus 48.1 degress Celsius for MqsR and 61.1 degress
CC Celsius for MqsA. {ECO:0000269|PubMed:23172222};
CC -!- SUBUNIT: Might be a dimer (PubMed:19690171). Also reported to be a
CC monomer (PubMed:23172222). Crystallizes as a heterotetramer with MqsA,
CC MqsR-MqsA(2)-MqsR (PubMed:20041169). Purifies as a possible
CC heterohexamer of 2 MqsR dimers and 1 MqsA dimer (PubMed:19690171). When
CC the 2 dissociate the MsqR mRNA interferase becomes active.
CC {ECO:0000269|PubMed:19690171, ECO:0000269|PubMed:20041169,
CC ECO:0000269|PubMed:23172222}.
CC -!- INDUCTION: Induced by amino acid starvation, glucose starvation and
CC when translation is blocked. Also induced by nalidixic acid,
CC azolocillin and H(2)O(2) (PubMed:23289863). It has been suggested that
CC MqsA represses its own operon (PubMed:19690171). Induction is decreased
CC in the absence of the Lon protease suggesting, by homology to other
CC toxin-antitoxin systems, that Lon may degrade the MqsA antitoxin.
CC Transcription is activated by MqsA (PubMed:20105222). A member of the
CC mqsRA operon. Most highly induced gene in persister cells
CC (PubMed:16768798). Degrades its own transcript (PubMed:23172222). This
CC operon induced by ectopic expression of toxins RelE, HicA and YafQ but
CC not by MazF or HicA (PubMed:23432955). {ECO:0000269|PubMed:16768798,
CC ECO:0000269|PubMed:20105222, ECO:0000269|PubMed:23172222,
CC ECO:0000269|PubMed:23289863, ECO:0000269|PubMed:23432955,
CC ECO:0000303|PubMed:19690171}.
CC -!- DISRUPTION PHENOTYPE: No loss of ability to form persister cells in
CC MG1655, represses persister cell formation in BW25113. Deletion
CC decreases biofilm formation in LB medium (PubMed:16352847). Deletion
CC has also been shown to increase biofilm formation (PubMed:20105222).
CC Deletion at 48h, in flow cells, leads to a reduction in biomass,
CC substratum coverage and changes the biofilm architecture from a 54
CC micron thick film with microcolonies to one with nearly no biomass and
CC only a few colonies remaining. Deletion abolishes motility. A double
CC mqsR-mqsA deletion leads to increased rpoS mRNA levels, resulting in
CC increased cyclic-di-GMP levels, increasing stress resistance, increased
CC biofilm formation (PubMed:21516113). The double mutant has increased
CC metabolism and respiration in the presence of the bile acid
CC deoxycholate and consequently grows less well. Decreases cell survival
CC in the presence of 20% deoxycholate (PubMed:25534751).
CC {ECO:0000269|PubMed:16352847, ECO:0000269|PubMed:16768798,
CC ECO:0000269|PubMed:19909729, ECO:0000269|PubMed:20105222,
CC ECO:0000269|PubMed:21516113, ECO:0000269|PubMed:25534751}.
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DR EMBL; U28377; AAA69190.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76058.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77078.1; -; Genomic_DNA.
DR PIR; D65089; D65089.
DR RefSeq; NP_417494.1; NC_000913.3.
DR RefSeq; WP_000415584.1; NZ_SSZK01000023.1.
DR PDB; 3HI2; X-ray; 2.00 A; B/D=1-98.
DR PDBsum; 3HI2; -.
DR AlphaFoldDB; Q46865; -.
DR SMR; Q46865; -.
DR BioGRID; 4260831; 22.
DR ComplexPortal; CPX-1084; MqsRA toxin-antitoxin complex.
DR IntAct; Q46865; 10.
DR STRING; 511145.b3022; -.
DR PaxDb; Q46865; -.
DR PRIDE; Q46865; -.
DR EnsemblBacteria; AAC76058; AAC76058; b3022.
DR EnsemblBacteria; BAE77078; BAE77078; BAE77078.
DR GeneID; 947500; -.
DR KEGG; ecj:JW2990; -.
DR KEGG; eco:b3022; -.
DR PATRIC; fig|1411691.4.peg.3708; -.
DR EchoBASE; EB2841; -.
DR eggNOG; ENOG5032TA0; Bacteria.
DR HOGENOM; CLU_161157_0_0_6; -.
DR OMA; IWQDVYH; -.
DR BioCyc; EcoCyc:G7572-MON; -.
DR BioCyc; MetaCyc:G7572-MON; -.
DR PRO; PR:Q46865; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0110001; C:toxin-antitoxin complex; IPI:ComplexPortal.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:EcoCyc.
DR GO; GO:0016892; F:endoribonuclease activity, producing 3'-phosphomonoesters; IDA:EcoCyc.
DR GO; GO:0061157; P:mRNA destabilization; IDA:EcoCyc.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:CACAO.
DR GO; GO:0017148; P:negative regulation of translation; IDA:EcoCyc.
DR GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-KW.
DR GO; GO:2000145; P:regulation of cell motility; IMP:CACAO.
DR GO; GO:0043488; P:regulation of mRNA stability; IDA:EcoCyc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0044010; P:single-species biofilm formation; IDA:ComplexPortal.
DR CDD; cd12869; MqsR; 1.
DR Gene3D; 3.30.2310.40; -; 1.
DR InterPro; IPR038493; MqsR_sf.
DR InterPro; IPR031451; MqsR_toxin.
DR Pfam; PF15723; MqsR_toxin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Nuclease; Quorum sensing;
KW Reference proteome; Stress response; Toxin-antitoxin system; Transcription;
KW Transcription regulation.
FT CHAIN 1..98
FT /note="mRNA interferase toxin MqsR"
FT /id="PRO_0000169411"
FT MUTAGEN 55
FT /note="Y->A: No change in toxicity."
FT /evidence="ECO:0000269|PubMed:20041169"
FT MUTAGEN 56
FT /note="K->A: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:20041169"
FT MUTAGEN 58
FT /note="M->A: No change in toxicity."
FT /evidence="ECO:0000269|PubMed:20041169"
FT MUTAGEN 68
FT /note="Q->A: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:20041169"
FT MUTAGEN 72
FT /note="R->A: No change in toxicity."
FT /evidence="ECO:0000269|PubMed:20041169"
FT MUTAGEN 81
FT /note="Y->A: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:20041169"
FT MUTAGEN 96
FT /note="K->A: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:20041169"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:3HI2"
FT HELIX 10..18
FT /evidence="ECO:0007829|PDB:3HI2"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:3HI2"
FT HELIX 26..34
FT /evidence="ECO:0007829|PDB:3HI2"
FT HELIX 39..47
FT /evidence="ECO:0007829|PDB:3HI2"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:3HI2"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:3HI2"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:3HI2"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:3HI2"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:3HI2"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:3HI2"
SQ SEQUENCE 98 AA; 11232 MW; D2662AB4DA8E111A CRC64;
MEKRTPHTRL SQVKKLVNAG QVRTTRSALL NADELGLDFD GMCNVIIGLS ESDFYKSMTT
YSDHTIWQDV YRPRLVTGQV YLKITVIHDV LIVSFKEK
