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RelB DNA-binding transcriptional repressor

Synonyms: RelB
RelB is the antitoxin of the RelE-RelB toxin-antitoxin system [2]. RelB also represses transcription of relBEF [2]. The RelE toxin inhibits protein translation by catalyzing cleavage of mRNA in the A site of the ribosome [3]. RelB production relieves established RelE-mediated translation inhibition and inhibition of cell growth, indicating that growth inhibition is not irreversible [4]. The activity of tmRNA, SsrA, counteracts RelE-mediated translation inhibition [3, 5].
The RelE-RelB system is involved in regulation of cell growth under conditions with limited nutrients [3, 5, 6, 7, 8]. A Tn10 insertion in ydfV restores colony-forming ability to an rne mutant.
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Transcription factor      
TF conformation(s):
Name Conformation Type TF-Effector Interaction Type Apo/Holo Conformation Evidence (Confirmed, Strong, Weak) References
RelB     nd nd
Evolutionary Family: RelB
Connectivity class: Local Regulator
Gene name: relB
  Genome position: 1645633-1645872
  Length: 240 bp / 79 aa
Operon name: relBE-hokD
TU(s) encoding the TF:
Transcription unit        Promoter
Gene name: relE
  Genome position: 1645346-1645633
  Length: 288 bp / 95 aa
Operon name: relBE-hokD
TU(s) encoding the TF:
Transcription unit        Promoter

Regulated gene(s) hokD, relB, relE
Multifun term(s) of regulated gene(s) MultiFun Term (List of genes associated to the multifun term)
RNA degradation (2)
translation attenuation and efficiency (2)
cell killing (2)
prophage genes and phage related functions (1)
Transcription related (1)
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Regulated operon(s) relBE-hokD
First gene in the operon(s) relB
Simple and complex regulons RelB
Simple and complex regulatory phrases Regulatory phrase (List of promoters regulated by the phrase)

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
  RelB repressor relBp Sigma70 1.5 -30.5 relB, relE, hokD
1645897 1645908 [BPP], [GEA], [HIBSCS] [1]
  RelB repressor relBp Sigma70 13.5 -18.5 relB, relE, hokD
1645885 1645896 [BPP], [GEA], [HIBSCS] [1]

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


 [BPP] Binding of purified proteins

 [GEA] Gene expression analysis

 [HIBSCS] Human inference based on similarity to consensus sequences


 [1] Li GY., Zhang Y., Inouye M., Ikura M., 2008, Structural mechanism of transcriptional autorepression of the Escherichia coli RelB/RelE antitoxin/toxin module., J Mol Biol. 380(1):107-19

 [2] Gotfredsen M., Gerdes K., 1998, The Escherichia coli relBE genes belong to a new toxin-antitoxin gene family., Mol Microbiol. 29(4):1065-76

 [3] Pedersen K., Zavialov AV., Pavlov MY., Elf J., Gerdes K., Ehrenberg M., 2003, The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site., Cell. 112(1):131-40

 [4] 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

 [5] Christensen SK., Gerdes K., 2003, RelE toxins from bacteria and Archaea cleave mRNAs on translating ribosomes, which are rescued by tmRNA., Mol Microbiol. 48(5):1389-400

 [6] Mosteller RD., 1978, Evidence that glucose starvation-sensitive mutants are altered in the relB locus., J Bacteriol. 133(2):1034-7

 [7] Diderichsen B., Desmarez L., 1980, Variations in phenotype of relB mutants of Escherichia coli and the effect of pus and sup mutations., Mol Gen Genet. 180(2):429-37

 [8] Christensen SK., Mikkelsen M., Pedersen K., Gerdes K., 2001, RelE, a global inhibitor of translation, is activated during nutritional stress., Proc Natl Acad Sci U S A. 98(25):14328-33

 [9] Tamura M., Kers JA., Cohen SN., 2012, Second-site suppression of RNase E essentiality by mutation of the deaD RNA helicase in Escherichia coli., J Bacteriol. 194(8):1919-26

 [10] Galvani C., Terry J., Ishiguro EE., 2001, Purification of the RelB and RelE proteins of Escherichia coli: RelE binds to RelB and to ribosomes., J Bacteriol. 183(8):2700-3

 [11] Bech FW., Jorgensen ST., Diderichsen B., Karlstrom OH., 1985, Sequence of the relB transcription unit from Escherichia coli and identification of the relB gene., EMBO J. 4(4):1059-66

 [12] Lavalle R., 1965, [New mutants for regulation of RNA synthesis], Bull Soc Chim Biol (Paris). 47(8):1567-70

 [13] Diderichsen B., Fiil NP., Lavalle R., 1977, Genetics of the relB locus in Escherichia coli., J Bacteriol. 131(1):30-3

 [14] Yamaguchi Y., Park JH., Inouye M., 2011, Toxin-antitoxin systems in bacteria and archaea., Annu Rev Genet. 45:61-79