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MazE DNA-binding transcriptional repressor

Synonyms: MazE
Summary:
MazE is an antitoxin that counteracts the MazF toxin [2, 3]. MazF exhibits ribonuclease activity toward single stranded RNA regions of sequence ACA, and the resulting degradation of cellular mRNA causes global translation inhibition [4]. MazF exhibits RNase activity toward tmRNA, and tmRNA is involved in release of MazF-mediated cell growth inhibition [5]. The mazEF system causes a "programmed cell death" response to stresses including starvation [3] and antibiotics [6]. The antitoxin, MazE, is subject to degradation by the ClpAP protease complex and exhibits a short (30 minute) half life, whereas the toxin, MazF, is much more stable [3].
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Transcription factor      
TF conformation(s):
Name Conformation Type TF-Effector Interaction Type Apo/Holo Conformation Evidence (Confirmed, Strong, Weak) References
MazE Functional   nd nd
Evolutionary Family: MazE
Connectivity class: Local Regulator
Gene name: mazE
  Genome position: 2911091-2911339
  Length: 249 bp / 82 aa
Operon name: relA-mazEFG
TU(s) encoding the TF:
Transcription unit        Promoter
mazEFG
mazEp1
mazEFG
mazEp2
relA-mazEF
relAp1
relA-mazEF
relAp2


Regulon       
Regulated gene(s) mazE, mazF, mazG
Multifun term(s) of regulated gene(s) MultiFun Term (List of genes associated to the multifun term)
starvation (3)
defense/survival (2)
other (mechanical, nutritional, oxidative stress) (2)
cell killing (2)
drug resistance/sensitivity (2)
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Regulated operon(s) relA-mazEFG
First gene in the operon(s) mazE
Simple and complex regulons Fis,MazE,MazE-MazF
Fis,MazE,MazE-MazF,ppGpp
Simple and complex regulatory phrases Regulatory phrase (List of promoters regulated by the phrase)
[MazE,-](2)


Transcription factor regulation    


Transcription factor binding sites (TFBSs) arrangements
      

  Functional conformation Function Promoter Sigma factor Central Rel-Pos Distance to first Gene Genes Sequence LeftPos RightPos Evidence (Confirmed, Strong, Weak) References
  MazE repressor mazEp1 nd -21.0 -50.0 mazE, mazF, mazG
gaaatttgctCGTATCTACAATGTAGATTGATATATACtgtatctaca
2911376 2911403 [BCE], [GEA], [SM], [BCE], [SM] [1]
  MazE repressor mazEp1 nd -7.0 -36.0 mazE, mazF, mazG
ctacaatgtaGATTGATATATACTGTATCTACATATgatagcggtt
2911363 2911388 [BCE], [GEA], [SM], [BCE], [SM] [1]
  MazE repressor mazEp2 nd -34.0 -50.0 mazE, mazF, mazG
gaaatttgctCGTATCTACAATGTAGATTGATATATACtgtatctaca
2911376 2911403 [GEA], [BCE], [SM] [1]
  MazE repressor mazEp2 nd -20.0 -36.0 mazE, mazF, mazG
ctacaatgtaGATTGATATATACTGTATCTACATATgatagcggtt
2911363 2911388 [GEA], [BCE], [SM] [1]


Evolutionary conservation of regulatory elements    
     Note: Evolutionary conservation of regulatory interactions and promoters is limited to gammaproteobacteria.
Promoter-target gene evolutionary conservation




Reference(s)    

 [1] Marianovsky I., Aizenman E., Engelberg-Kulka H., Glaser G., 2001, The regulation of the Escherichia coli mazEF promoter involves an unusual alternating palindrome., J Biol Chem 276(8):5975-84

 [2] Masuda Y., Miyakawa K., Nishimura Y., Ohtsubo E., 1993, chpA and chpB, Escherichia coli chromosomal homologs of the pem locus responsible for stable maintenance of plasmid R100., J Bacteriol 175(21):6850-6

 [3] Aizenman E., Engelberg-Kulka H., Glaser G., 1996, An Escherichia coli chromosomal "addiction module" regulated by guanosine [corrected] 3',5'-bispyrophosphate: a model for programmed bacterial cell death., Proc Natl Acad Sci U S A 93(12):6059-63

 [4] Zhang Y, Zhang J, Hoeflich KP, Ikura M, Qing G, Inouye M, 2003, MazF cleaves cellular mRNAs specifically at ACA to block protein synthesis in Escherichia coli., Mol Cell, 12(4):913 10.1016/s1097-2765(03)00402-7

 [5] Christensen SK, Pedersen K, Hansen FG, Gerdes K, 2003, Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA., J Mol Biol, 332(4):809 10.1016/s0022-2836(03)00922-7

 [6] Sat B, Hazan R, Fisher T, Khaner H, Glaser G, Engelberg-Kulka H, 2001, Programmed cell death in Escherichia coli: some antibiotics can trigger mazEF lethality., J Bacteriol, 183(6):2041 10.1128/JB.183.6.2041-2045.2001

 [7] Pedersen K, Christensen SK, Gerdes K, 2002, Rapid induction and reversal of a bacteriostatic condition by controlled expression of toxins and antitoxins., Mol Microbiol, 45(2):501 10.1046/j.1365-2958.2002.03027.x

 [8] Sat B, Reches M, Engelberg-Kulka H, 2003, The Escherichia coli mazEF suicide module mediates thymineless death., J Bacteriol, 185(6):1803 10.1128/JB.185.6.1803-1807.2003

 [9] Kamada K, Hanaoka F, Burley SK, 2003, Crystal structure of the MazE/MazF complex: molecular bases of antidote-toxin recognition., Mol Cell, 11(4):875 10.1016/s1097-2765(03)00097-2

 [10] Zhang J, Zhang Y, Inouye M, 2003, Characterization of the interactions within the mazEF addiction module of Escherichia coli., J Biol Chem, 278(34):32300 10.1074/jbc.M304767200

 [11] Lah J, Marianovsky I, Glaser G, Engelberg-Kulka H, Kinne J, Wyns L, Loris R, 2003, Recognition of the intrinsically flexible addiction antidote MazE by a dromedary single domain antibody fragment. Structure, thermodynamics of binding, stability, and influence on interactions with DNA., J Biol Chem, 278(16):14101 10.1074/jbc.M209855200

 [12] Loris R, Marianovsky I, Lah J, Laeremans T, Engelberg-Kulka H, Glaser G, Muyldermans S, Wyns L, 2003, Crystal structure of the intrinsically flexible addiction antidote MazE., J Biol Chem, 278(30):28252 10.1074/jbc.M302336200

 [13] Mittenhuber G, 1999, Occurrence of mazEF-like antitoxin/toxin systems in bacteria., J Mol Microbiol Biotechnol, 1(2):295 None

 [14] Santos-Sierra S, Giraldo R, Díaz-Orejas R, 1997, Functional interactions between homologous conditional killer systems of plasmid and chromosomal origin., FEMS Microbiol Lett, 152(1):51 10.1111/j.1574-6968.1997.tb10408.x

 [15] Engelberg-Kulka H, Reches M, Narasimhan S, Schoulaker-Schwarz R, Klemes Y, Aizenman E, Glaser G, 1998, rexB of bacteriophage lambda is an anti-cell death gene., Proc Natl Acad Sci U S A, 95(26):15481 10.1073/pnas.95.26.15481

 [16] Metzger S., Dror IB., Aizenman E., Schreiber G., Toone M., Friesen JD., Cashel M., Glaser G., 1988, The nucleotide sequence and characterization of the relA gene of Escherichia coli., J Biol Chem 263(30):15699-704

 [17] de la Cueva-Méndez G, 2003, Distressing bacteria: structure of a prokaryotic detox program., Mol Cell, 11(4):848 10.1016/s1097-2765(03)00146-1

 [18] Yamaguchi Y, Park JH, Inouye M, 2011, Toxin-antitoxin systems in bacteria and archaea., Annu Rev Genet, 45(None):61 10.1146/annurev-genet-110410-132412



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