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P0C077 (RELE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
mRNA interferase RelE

EC=3.1.-.-
Alternative name(s):
Endoribonuclease RelE
Toxin RelE
Gene names
Name:relE
Ordered Locus Names:b1563, JW1555
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length95 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Toxic component of a toxin-antitoxin (TA) module. A sequence-specific, ribosome-dependent mRNA endoribonuclease that inhibits translation during amino acid starvation (the stringent response). Acts by cleaving mRNA with high codon specificity in the ribosomal A site between positions 2 and 3. The stop codon UAG is cleaved at a fast rate while UAA and UGA are cleaved with intermediate and slow rates. mRNA cleavage can also occur in the ribosomal E site after peptide release from peptidyl-tRNA in the P site as well as on free 30S subunits. Overexpression of RelE results in the inhibition of bacterial growth and a sharp decrease in colony-forming ability which is inhibited by the labile cognate antitoxin RelB. Overexpression also sharply increases persisters (cells that neither grow or die in presence of bactericidal agent and are largely responsible for high levels of biofilm tolerance to antimicrobials). Acts with RelB as a corepressor of relBE transcription. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11

Seems to be a principal mediator of cell death in liquid media. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11

Subunit structure

Binds DNA as a RelE(2)-RelB2 heterotetramer. RelE occupies the A site of the 70S ribosome, making extensive contacts with the 16S rRNA. Its presence blocks access of tRNAs and translation factors. RelB inhibits its endonuclease activity. Ref.6 Ref.12

Induction

By amino acid starvation, by glucose starvation and by chloramphenicol. Induction is independent of ppGpp. Member of the relBE operon. Ref.7

Disruption phenotype

Cells missing relBE have a higher steady-state level of translation during amino acid starvation than wild-type cells. They survive antibiotic treatment in log phase better than wild-type cells. Ref.7 Ref.11

Sequence similarities

Belongs to the RelE toxin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9595mRNA interferase RelE
PRO_0000097245

Experimental info

Mutagenesis611R → A: Greatly decreased mRNA cleavage. Ref.14
Mutagenesis81 – 833RER → AEA: Significant reduction in endonuclease activity, still binds RelB. Ref.8 Ref.14
Mutagenesis811R → A: Significantly decreased mRNA cleavage, significantly less translation inhibition which is countered by RelB. Almost complete loss of mRNA cleavage; when associated with F-87. Ref.8 Ref.14
Mutagenesis871Y → A: Significantly decreased mRNA cleavage. Ref.14
Mutagenesis871Y → F: No effect on mRNA cleavage, almost complete loss; when associated with A-81. Ref.14
Mutagenesis90 – 956AVKRIL → VTVTVT: Does not inhibit translation. Ref.8

Secondary structure

...................... 95
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0C077 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: F516B2E7A437CCEC

FASTA9511,225
        10         20         30         40         50         60 
MAYFLDFDER ALKEWRKLGS TVREQLKKKL VEVLESPRIE ANKLRGMPDC YKIKLRSSGY 

        70         80         90 
RLVYQVIDEK VVVFVISVGK RERSEVYSEA VKRIL 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of the relB transcription unit from Escherichia coli and identification of the relB gene."
Bech F.W., Joergensen S.T., Diderichsen B., Karlstroem O.H.
EMBO J. 4:1059-1066(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / CS520.
[2]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"The Escherichia coli relBE genes belong to a new toxin-antitoxin gene family."
Gotfredsen M., Gerdes K.
Mol. Microbiol. 29:1065-1076(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A TOXIN, FUNCTION AS A TRANSCRIPTIONAL COREPRESSOR.
[6]"Purification of the RelB and RelE proteins of Escherichia coli: RelE binds to RelB and to ribosomes."
Galvani C., Terry J., Ishiguro E.E.
J. Bacteriol. 183:2700-2703(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, RIBOSOME-BINDING.
[7]"RelE, a global inhibitor of translation, is activated during nutritional stress."
Christensen S.K., Mikkelsen M., Pedersen K., Gerdes K.
Proc. Natl. Acad. Sci. U.S.A. 98:14328-14333(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A TRANSLATION INHIBITOR, INDUCTION, DISRUPTION PHENOTYPE.
[8]"Rapid induction and reversal of a bacteriostatic condition by controlled expression of toxins and antitoxins."
Pedersen K., Christensen S.K., Gerdes K.
Mol. Microbiol. 45:501-510(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A TOXIN, MUTAGENESIS OF ARG-81 AND 90-ALA--LEU-95.
Strain: K12.
[9]"The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site."
Pedersen K., Zavialov A.V., Pavlov M.Y., Elf J., Gerdes K., Ehrenberg M.
Cell 112:131-140(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS AN ENDORIBONUCLEASE ON THE RIBOSOME.
[10]"Specialized persister cells and the mechanism of multidrug tolerance in Escherichia coli."
Keren I., Shah D., Spoering A., Kaldalu N., Lewis K.
J. Bacteriol. 186:8172-8180(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: RELATION WITH PERSISTERS.
[11]"A differential effect of E. coli toxin-antitoxin systems on cell death in liquid media and biofilm formation."
Kolodkin-Gal I., Verdiger R., Shlosberg-Fedida A., Engelberg-Kulka H.
PLoS ONE 4:E6785-E6785(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL DEATH, DISRUPTION PHENOTYPE.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[12]"Structural mechanism of transcriptional autorepression of the Escherichia coli RelB/RelE antitoxin/toxin module."
Li G.Y., Zhang Y., Inouye M., Ikura M.
J. Mol. Biol. 380:107-119(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[13]"mRNA interferases, sequence-specific endoribonucleases from the toxin-antitoxin systems."
Yamaguchi Y., Inouye M.
Prog. Mol. Biol. Transl. Sci. 85:467-500(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[14]"The structural basis for mRNA recognition and cleavage by the ribosome-dependent endonuclease RelE."
Neubauer C., Gao Y.G., Andersen K.R., Dunham C.M., Kelley A.C., Hentschel J., Gerdes K., Ramakrishnan V., Brodersen D.E.
Cell 139:1084-1095(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN ISOLATION AND BOUND TO RIBOSOMES BEFORE AND AFTER MRNA CLEAVAGE, RIBOSOME-BINDING, RRNA-BINDING, MECHANISM OF CLEAVAGE, MUTAGENESIS OF ARG-61; ARG-81 AND TYR-87.
[15]"Inhibitory mechanism of Escherichia coli RelE-RelB toxin-antitoxin module involves a helix displacement near an mRNA interferase active site."
Li G.Y., Zhang Y., Inouye M., Ikura M.
J. Biol. Chem. 284:14628-14636(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF MUTANT 81-ARG--ARG-83 IN COMPLEX WITH RELB FRAGMENT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02405 Genomic DNA. Translation: CAA26251.1.
U00096 Genomic DNA. Translation: AAC74636.1.
AP009048 Genomic DNA. Translation: BAA15262.1.
PIRQQECR1. B22830.
RefSeqNP_416081.1. NC_000913.3.
YP_489827.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KC8NMR-A1-95[»]
2KC9NMR-A1-95[»]
3KIQX-ray3.30y1-95[»]
3KISX-ray3.30y1-95[»]
3KIUX-ray3.60y1-95[»]
3KIXX-ray3.60y1-95[»]
4FXEX-ray2.75D/E/F1-95[»]
4FXHX-ray2.40A/B1-95[»]
4FXIX-ray2.50A/B/C1-95[»]
ProteinModelPortalP0C077.
SMRP0C077. Positions 2-95.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35978N.
IntActP0C077. 11 interactions.
MINTMINT-1282331.
STRING511145.b1563.

Proteomic databases

PaxDbP0C077.
PRIDEP0C077.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74636; AAC74636; b1563.
BAA15262; BAA15262; BAA15262.
GeneID12931249.
947549.
KEGGecj:Y75_p1539.
eco:b1563.
PATRIC32118432. VBIEscCol129921_1636.

Organism-specific databases

EchoBASEEB1121.
EcoGeneEG11131. relE.

Phylogenomic databases

eggNOGCOG2026.
HOGENOMHOG000219994.
KOK06218.
OMAGHADRYK.
OrthoDBEOG6S52Q2.

Enzyme and pathway databases

BioCycEcoCyc:EG11131-MONOMER.
ECOL316407:JW1555-MONOMER.
MetaCyc:EG11131-MONOMER.

Gene expression databases

GenevestigatorP0C077.

Family and domain databases

InterProIPR007712. RelE/ParE_toxin.
[Graphical view]
PfamPF05016. Plasmid_stabil. 1 hit.
[Graphical view]
TIGRFAMsTIGR02385. RelE_StbE. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0C077.
PROP0C077.

Entry information

Entry nameRELE_ECOLI
AccessionPrimary (citable) accession number: P0C077
Secondary accession number(s): P07008
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: June 11, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene