Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0C077

- RELE_ECOLI

UniProt

P0C077 - RELE_ECOLI

Protein

mRNA interferase RelE

Gene

relE

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    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.
    Seems to be a principal mediator of cell death in liquid media.

    GO - Molecular functioni

    1. endoribonuclease activity Source: EcoCyc
    2. protein binding Source: EcoCyc
    3. ribosome binding Source: EcoCyc
    4. rRNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. cellular response to amino acid starvation Source: EcoCyc
    2. mRNA catabolic process Source: EcoCyc
    3. negative regulation of translation Source: EcoCyc
    4. regulation of transcription, DNA-templated Source: UniProtKB-KW
    5. response to antibiotic Source: EcoCyc
    6. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease, Repressor, Toxin

    Keywords - Biological processi

    Stress response, Transcription, Transcription regulation

    Keywords - Ligandi

    RNA-binding, rRNA-binding

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    mRNA interferase RelE (EC:3.1.-.-)
    Alternative name(s):
    Endoribonuclease RelE
    Toxin RelE
    Gene namesi
    Name:relE
    Ordered Locus Names:b1563, JW1555
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11131. relE.

    Pathology & Biotechi

    Disruption phenotypei

    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.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi61 – 611R → A: Greatly decreased mRNA cleavage. 1 Publication
    Mutagenesisi81 – 833RER → AEA: Significant reduction in endonuclease activity, still binds RelB. 2 Publications
    Mutagenesisi81 – 811R → 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. 2 Publications
    Mutagenesisi87 – 871Y → A: Significantly decreased mRNA cleavage. 1 Publication
    Mutagenesisi87 – 871Y → F: No effect on mRNA cleavage, almost complete loss; when associated with A-81. 1 Publication
    Mutagenesisi90 – 956AVKRIL → VTVTVT: Does not inhibit translation.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 9595mRNA interferase RelEPRO_0000097245Add
    BLAST

    Proteomic databases

    PaxDbiP0C077.
    PRIDEiP0C077.

    Expressioni

    Inductioni

    By amino acid starvation, by glucose starvation and by chloramphenicol. Induction is independent of ppGpp. Member of the relBE operon.1 Publication

    Gene expression databases

    GenevestigatoriP0C077.

    Interactioni

    Subunit structurei

    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.3 Publications

    Protein-protein interaction databases

    DIPiDIP-35978N.
    IntActiP0C077. 11 interactions.
    MINTiMINT-1282331.
    STRINGi511145.b1563.

    Structurei

    Secondary structure

    1
    95
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 74
    Helixi9 – 179
    Helixi20 – 3516
    Helixi40 – 423
    Beta strandi45 – 473
    Beta strandi50 – 545
    Turni56 – 594
    Beta strandi60 – 678
    Helixi68 – 703
    Beta strandi72 – 809
    Helixi82 – 843
    Helixi85 – 9410

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP0C077.
    SMRiP0C077. Positions 2-95.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0C077.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RelE toxin family.Curated

    Phylogenomic databases

    eggNOGiCOG2026.
    HOGENOMiHOG000219994.
    KOiK06218.
    OMAiGHADRYK.
    OrthoDBiEOG6S52Q2.

    Family and domain databases

    InterProiIPR007712. RelE/ParE_toxin.
    [Graphical view]
    PfamiPF05016. Plasmid_stabil. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR02385. RelE_StbE. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0C077-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAYFLDFDER ALKEWRKLGS TVREQLKKKL VEVLESPRIE ANKLRGMPDC   50
    YKIKLRSSGY RLVYQVIDEK VVVFVISVGK RERSEVYSEA VKRIL 95
    Length:95
    Mass (Da):11,225
    Last modified:April 1, 1988 - v1
    Checksum:iF516B2E7A437CCEC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02405 Genomic DNA. Translation: CAA26251.1.
    U00096 Genomic DNA. Translation: AAC74636.1.
    AP009048 Genomic DNA. Translation: BAA15262.1.
    PIRiB22830. QQECR1.
    RefSeqiNP_416081.1. NC_000913.3.
    YP_489827.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74636; AAC74636; b1563.
    BAA15262; BAA15262; BAA15262.
    GeneIDi12931249.
    947549.
    KEGGiecj:Y75_p1539.
    eco:b1563.
    PATRICi32118432. VBIEscCol129921_1636.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02405 Genomic DNA. Translation: CAA26251.1 .
    U00096 Genomic DNA. Translation: AAC74636.1 .
    AP009048 Genomic DNA. Translation: BAA15262.1 .
    PIRi B22830. QQECR1.
    RefSeqi NP_416081.1. NC_000913.3.
    YP_489827.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KC8 NMR - A 1-95 [» ]
    2KC9 NMR - A 1-95 [» ]
    3KIQ X-ray 3.30 y 1-95 [» ]
    3KIS X-ray 3.30 y 1-95 [» ]
    3KIU X-ray 3.60 y 1-95 [» ]
    3KIX X-ray 3.60 y 1-95 [» ]
    4FXE X-ray 2.75 D/E/F 1-95 [» ]
    4FXH X-ray 2.40 A/B 1-95 [» ]
    4FXI X-ray 2.50 A/B/C 1-95 [» ]
    ProteinModelPortali P0C077.
    SMRi P0C077. Positions 2-95.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35978N.
    IntActi P0C077. 11 interactions.
    MINTi MINT-1282331.
    STRINGi 511145.b1563.

    Proteomic databases

    PaxDbi P0C077.
    PRIDEi P0C077.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74636 ; AAC74636 ; b1563 .
    BAA15262 ; BAA15262 ; BAA15262 .
    GeneIDi 12931249.
    947549.
    KEGGi ecj:Y75_p1539.
    eco:b1563.
    PATRICi 32118432. VBIEscCol129921_1636.

    Organism-specific databases

    EchoBASEi EB1121.
    EcoGenei EG11131. relE.

    Phylogenomic databases

    eggNOGi COG2026.
    HOGENOMi HOG000219994.
    KOi K06218.
    OMAi GHADRYK.
    OrthoDBi EOG6S52Q2.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG11131-MONOMER.
    ECOL316407:JW1555-MONOMER.
    MetaCyc:EG11131-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0C077.
    PROi P0C077.

    Gene expression databases

    Genevestigatori P0C077.

    Family and domain databases

    InterProi IPR007712. RelE/ParE_toxin.
    [Graphical view ]
    Pfami PF05016. Plasmid_stabil. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR02385. RelE_StbE. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. 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.

    Entry informationi

    Entry nameiRELE_ECOLI
    AccessioniPrimary (citable) accession number: P0C077
    Secondary accession number(s): P07008
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: April 1, 1988
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3