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P21513

- RNE_ECOLI

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Protein
Ribonuclease E
Gene
rne, ams, hmp1, b1084, JW1071

Gene:

rne, ams, hmp1, b1084, JW1071
Organism
Escherichia coli (strain K12)
Status
Reviewed - - Experimental evidence at protein leveli

UniProt

P21513 - RNE_ECOLI

Protein:

Ribonuclease E
Protein Existence: Experimental evidence at protein level

Functioni

Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs. Can also process other RNA species, such as RNAI, a molecule that controls the replication of ColE1 plasmid, and the cell division inhibitor DicF-RNA. It initiates the decay of RNAs by cutting them internally near their 5'-end. It is able to remove poly(A) tails by an endonucleolytic process.9 Publications

Catalytic activityi

Endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions.3 Publications

Cofactori

Binds 2 Zn2+ ions per homotetramer. Zinc ions are bound betweeen subunits and are essential for homotetramerization and catalytic activity, but not for RNA binding. In the absence of zinc, the protein dissociates into inactive dimers.2 Publications
Binds 1 Mg2+ ion per subunit.2 Publications

Enzyme regulationi

Binding to the membrane stabilizes protein structure and increases affinity for the substrate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Metal bindingi3031Magnesium; catalytic
Metal bindingi3461Magnesium; catalytic
Metal bindingi4041Zinc; shared with dimeric partner
Metal bindingi4071Zinc; shared with dimeric partner

GO - Molecular functioni

  1. RNA bindingInferred from electronic annotationi Source: UniProtKB-HAMAP
  2. endoribonuclease activityInferred from electronic annotationi Source: UniProtKB-HAMAP
  3. magnesium ion bindingInferred from electronic annotationi Source: UniProtKB-HAMAP
  4. zinc ion bindingInferred from electronic annotationi Source: UniProtKB-HAMAP
Complete GO annotation...

GO - Biological processi

  1. RNA bindingInferred from electronic annotationi Source: UniProtKB-HAMAP
  2. endoribonuclease activityInferred from electronic annotationi Source: UniProtKB-HAMAP
  3. magnesium ion bindingInferred from electronic annotationi Source: UniProtKB-HAMAP
  4. zinc ion bindingInferred from electronic annotationi Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

rRNA processing, tRNA processing

Keywords - Ligandi

Magnesium, Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG10859-MONOMER.
ECOL316407:JW1071-MONOMER.
MetaCyc:EG10859-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease E (EC:3.1.26.12)
Short name:
RNase E
Gene namesi
Name:rne
Synonyms:ams, hmp1
Ordered Locus Names:b1084, JW1071
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10859. rne.

Subcellular locationi

Cytoplasm. Cell inner membrane; Peripheral membrane protein; Cytoplasmic side
Note: Associated with the cytoplasmic membrane via the N- and C-terminal regions.1 Publication

GO - Cellular componenti

  1. cytoplasmInferred from direct assayi PubMed 9501232 Source: EcoCyc
  2. cytoplasmic side of plasma membraneInferred from electronic annotationi Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Mutagenesisi571F → A: Reduces RNA cleavage by over 98%. 1 Publication
Mutagenesisi661G → S: Disrupts folding of the S1 motif. 1 Publication
Mutagenesisi671F → A: Reduces RNA cleavage by over 98%. Reduces affinity for RNA. 1 Publication
Mutagenesisi1121K → A: Reduces RNA cleavage by 98%. Loss of RNA-binding. 1 Publication
Mutagenesisi1701T → V: Abolishes enzyme activity toward RNA substrates with a 5' monophosphate (PubMed:16237448). Strongly reduces enzyme activity toward cspA mRNA (PubMed:19889093). 2 Publications
Mutagenesisi3031D → N: Reduces RNA cleavage by over 96%. 1 Publication
Mutagenesisi3051N → D or L: Reduces RNA cleavage by over 96%. 1 Publication
Mutagenesisi3461D → N: Reduces RNA cleavage by over 96%. Reduces affinity for RNA. 1 Publication
Mutagenesisi3731R → A or D: Reduces RNA cleavage by 89%. 1 Publication
Mutagenesisi4041C → A: Reduces zinc-binding. Abolishes homotetramerization and enzyme activity. 1 Publication
Mutagenesisi4071C → A: Reduces zinc-binding. Abolishes homotetramerization and enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Chaini1 – 10611061Ribonuclease EUniRule annotation
PRO_0000097373

Proteomic databases

PaxDbiP21513.
PRIDEiP21513.

Expressioni

Gene expression databases

GenevestigatoriP21513.

Interactioni

Subunit structurei

Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation. Within the RNA degradosome, Rnase E assembles into a homotetramer formed by a dimer of dimers. Tetramerization is essential for catalytic activity, but not for RNA-binding. Interacts with RhlB, PNPase (pnp) and enolase (eno). Interacts with DeaD at reduced temperature.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
dnaKP0A6Y89EBI-549958,EBI-542092
enoP0A6P915EBI-549958,EBI-368855
pnpP0505511EBI-549958,EBI-548080
rhlBP0A8J816EBI-549958,EBI-555806

Protein-protein interaction databases

DIPiDIP-10727N.
IntActiP21513. 61 interactions.
MINTiMINT-1220086.
STRINGi511145.b1084.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Beta strandi2 – 76
Beta strandi10 – 123
Beta strandi14 – 207
Beta strandi23 – 308
Beta strandi32 – 343
Beta strandi36 – 394
Beta strandi42 – 509
Helixi51 – 533
Beta strandi55 – 6410
Beta strandi66 – 694
Helixi70 – 723
Helixi75 – 773
Beta strandi84 – 863
Helixi90 – 923
Beta strandi99 – 1068
Beta strandi110 – 1123
Beta strandi115 – 1184
Beta strandi125 – 1306
Beta strandi134 – 1363
Turni145 – 1484
Helixi151 – 1555
Beta strandi165 – 1684
Helixi170 – 1745
Helixi177 – 19923
Beta strandi205 – 2084
Beta strandi210 – 2123
Helixi213 – 2219
Beta strandi226 – 2327
Helixi234 – 24613
Helixi250 – 2556
Beta strandi256 – 2583
Helixi265 – 2684
Helixi272 – 2776
Beta strandi281 – 2844
Beta strandi290 – 2956
Beta strandi300 – 3056
Helixi315 – 33622
Beta strandi341 – 3466
Helixi353 – 36614
Turni367 – 3693
Beta strandi374 – 3796
Beta strandi383 – 3897
Helixi396 – 4005
Beta strandi405 – 4117
Helixi416 – 43217
Beta strandi436 – 4438
Helixi445 – 4517
Turni452 – 4554
Helixi456 – 46510
Turni466 – 4683
Beta strandi470 – 4756
Beta strandi485 – 4906
Turni491 – 4933
Helixi499 – 5013
Helixi502 – 5065
Turni507 – 5093
Helixi831 – 8333
Helixi835 – 8384

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SLJNMR-A35-125[»]
1SMXX-ray1.80A/B35-125[»]
1SN8X-ray2.00A/B35-125[»]
2BX2X-ray2.85L1-510[»]
2C0BX-ray3.18L1-510[»]
2C4RX-ray3.60L1-510[»]
2FYMX-ray1.60B/E833-850[»]
2VMKX-ray3.30A/B/C/D1-515[»]
2VRTX-ray3.50A/B/C/D1-509[»]
3GCMX-ray2.50D/E/F1021-1061[»]
3GMEX-ray2.40D1021-1061[»]
3H1CX-ray3.57D/E/F/H/J/L/N/P/S/U/W/Y1021-1061[»]
3H8AX-ray1.90E/F823-850[»]
DisProtiDP00207.
ProteinModelPortaliP21513.
SMRiP21513. Positions 1-510, 823-850.

Miscellaneous databases

EvolutionaryTraceiP21513.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Domaini39 – 11981S1 motif

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Regioni57 – 11256Interaction with RNAUniRule annotation
Regioni169 – 1702Interaction with RNA 5'-terminal monophosphateUniRule annotation
Regioni404 – 4074Required for zinc-mediated homotetramerization and catalytic activityUniRule annotation
Regioni833 – 85018Interaction with enolaseUniRule annotation
Regioni1021 – 106141Interaction with PNPaseUniRule annotation

Domaini

The N-terminal S1 motif binds RNA, and can also bind single-stranded DNA (in vitro). The C-terminal region interacts with the other degradosomal components.2 Publications

Sequence similaritiesi

Contains 1 S1 motif domain.

Phylogenomic databases

eggNOGiCOG1530.
HOGENOMiHOG000258027.
KOiK08300.
OMAiENTKEVH.
OrthoDBiEOG6PCPTH.
ProtClustDBiPRK10811.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00970. RNase_E.
InterProiIPR012340. NA-bd_OB-fold.
IPR021968. PNPase_C.
IPR003029. Rbsml_prot_S1_RNA-bd_dom.
IPR019307. RNA-bd_AU-1/RNase_E/G.
IPR022967. RNA-binding_domain_S1.
IPR028878. RNase_E.
IPR004659. RNase_E/G.
[Graphical view]
PfamiPF12111. PNPase_C. 1 hit.
PF10150. RNase_E_G. 1 hit.
PF00575. S1. 1 hit.
[Graphical view]
SMARTiSM00316. S1. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00757. RNaseEG. 1 hit.
PROSITEiPS50126. S1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P21513-1 [UniParc]FASTA

« Hide

MKRMLINATQ QEELRVALVD GQRLYDLDIE SPGHEQKKAN IYKGKITRIE     50
PSLEAAFVDY GAERHGFLPL KEIAREYFPA NYSAHGRPNI KDVLREGQEV 100
IVQIDKEERG NKGAALTTFI SLAGSYLVLM PNNPRAGGIS RRIEGDDRTE 150
LKEALASLEL PEGMGLIVRT AGVGKSAEAL QWDLSFRLKH WEAIKKAAES 200
RPAPFLIHQE SNVIVRAFRD YLRQDIGEIL IDNPKVLELA RQHIAALGRP 250
DFSSKIKLYT GEIPLFSHYQ IESQIESAFQ REVRLPSGGS IVIDSTEALT 300
AIDINSARAT RGGDIEETAF NTNLEAADEI ARQLRLRDLG GLIVIDFIDM 350
TPVRHQRAVE NRLREAVRQD RARIQISHIS RFGLLEMSRQ RLSPSLGESS 400
HHVCPRCSGT GTVRDNESLS LSILRLIEEE ALKENTQEVH AIVPVPIASY 450
LLNEKRSAVN AIETRQDGVR CVIVPNDQME TPHYHVLRVR KGEETPTLSY 500
MLPKLHEEAM ALPSEEEFAE RKRPEQPALA TFAMPDVPPA PTPAEPAAPV 550
VAPAPKAAPA TPAAPAQPGL LSRFFGALKA LFSGGEETKP TEQPAPKAEA 600
KPERQQDRRK PRQNNRRDRN ERRDTRSERT EGSDNREENR RNRRQAQQQT 650
AETRESRQQA EVTEKARTAD EQQAPRRERS RRRNDDKRQA QQEAKALNVE 700
EQSVQETEQE ERVRPVQPRR KQRQLNQKVR YEQSVAEEAV VAPVVEETVA 750
AEPIVQEAPA PRTELVKVPL PVVAQTAPEQ QEENNADNRD NGGMPRRSRR 800
SPRHLRVSGQ RRRRYRDERY PTQSPMPLTV ACASPELASG KVWIRYPIVR 850
PQDVQVEEQR EQEEVHVQPM VTEVPVAAAI EPVVSAPVVE EVAGVVEAPV 900
QVAEPQPEVV ETTHPEVIAA AVTEQPQVIT ESDVAVAQEV AEQAEPVVEP 950
QEETADIEEV VETAEVVVAE PEVVAQPAAP VVAEVAAEVE TVAAVEPEVT 1000
VEHNHATAPM TRAPAPEYVP EAPRHSDWQR PTFAFEGKGA AGGHTATHHA 1050
SAAPARPQPV E 1061
Length:1,061
Mass (Da):118,197
Last modified:August 29, 2003 - v6
Checksum:iD4066D80E1DE7D37
GO

Sequence conflict

The sequence AAA23443.1 differs from that shown. Reason: Frameshift at position 796.
The sequence CAA38206.1 differs from that shown. Reason: Frameshift at several positions.
The sequence CAA47818.1 differs from that shown. Reason: Frameshift at position 1003.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Sequence conflicti3901Q → H in AAA23443. 1 Publication
Sequence conflicti4871L → V in CAA47818. 1 Publication
Sequence conflicti4871L → V in AAA23443. 1 Publication
Sequence conflicti5641A → R in CAA47818. 1 Publication
Sequence conflicti7841N → K in CAA47818. 1 Publication
Sequence conflicti8381A → R in AAA23443. 1 Publication
Sequence conflicti9051P → R in CAA47818. 1 Publication
Sequence conflicti10481H → R in AAA03347. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00096 Genomic DNA. Translation: AAC74168.1.
AP009048 Genomic DNA. Translation: BAA35893.1.
X67470 Genomic DNA. Translation: CAA47818.1. Frameshift.
M62747 Genomic DNA. Translation: AAA23443.1. Frameshift.
X54309 Genomic DNA. Translation: CAA38206.1. Frameshift.
L23942 Genomic DNA. Translation: AAA03347.1.
PIRiS27311. A64852.
RefSeqiNP_415602.1. NC_000913.3.
YP_489352.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74168; AAC74168; b1084.
BAA35893; BAA35893; BAA35893.
GeneIDi12932029.
945641.
KEGGiecj:Y75_p1054.
eco:b1084.
PATRICi32117409. VBIEscCol129921_1127.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00096 Genomic DNA. Translation: AAC74168.1 .
AP009048 Genomic DNA. Translation: BAA35893.1 .
X67470 Genomic DNA. Translation: CAA47818.1 . Frameshift.
M62747 Genomic DNA. Translation: AAA23443.1 . Frameshift.
X54309 Genomic DNA. Translation: CAA38206.1 . Frameshift.
L23942 Genomic DNA. Translation: AAA03347.1 .
PIRi S27311. A64852.
RefSeqi NP_415602.1. NC_000913.3.
YP_489352.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1SLJ NMR - A 35-125 [» ]
1SMX X-ray 1.80 A/B 35-125 [» ]
1SN8 X-ray 2.00 A/B 35-125 [» ]
2BX2 X-ray 2.85 L 1-510 [» ]
2C0B X-ray 3.18 L 1-510 [» ]
2C4R X-ray 3.60 L 1-510 [» ]
2FYM X-ray 1.60 B/E 833-850 [» ]
2VMK X-ray 3.30 A/B/C/D 1-515 [» ]
2VRT X-ray 3.50 A/B/C/D 1-509 [» ]
3GCM X-ray 2.50 D/E/F 1021-1061 [» ]
3GME X-ray 2.40 D 1021-1061 [» ]
3H1C X-ray 3.57 D/E/F/H/J/L/N/P/S/U/W/Y 1021-1061 [» ]
3H8A X-ray 1.90 E/F 823-850 [» ]
DisProti DP00207.
ProteinModelPortali P21513.
SMRi P21513. Positions 1-510, 823-850.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-10727N.
IntActi P21513. 61 interactions.
MINTi MINT-1220086.
STRINGi 511145.b1084.

Proteomic databases

PaxDbi P21513.
PRIDEi P21513.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74168 ; AAC74168 ; b1084 .
BAA35893 ; BAA35893 ; BAA35893 .
GeneIDi 12932029.
945641.
KEGGi ecj:Y75_p1054.
eco:b1084.
PATRICi 32117409. VBIEscCol129921_1127.

Organism-specific databases

EchoBASEi EB0852.
EcoGenei EG10859. rne.

Phylogenomic databases

eggNOGi COG1530.
HOGENOMi HOG000258027.
KOi K08300.
OMAi ENTKEVH.
OrthoDBi EOG6PCPTH.
ProtClustDBi PRK10811.

Enzyme and pathway databases

BioCyci EcoCyc:EG10859-MONOMER.
ECOL316407:JW1071-MONOMER.
MetaCyc:EG10859-MONOMER.

Miscellaneous databases

EvolutionaryTracei P21513.
PROi P21513.

Gene expression databases

Genevestigatori P21513.

Family and domain databases

Gene3Di 2.40.50.140. 1 hit.
HAMAPi MF_00970. RNase_E.
InterProi IPR012340. NA-bd_OB-fold.
IPR021968. PNPase_C.
IPR003029. Rbsml_prot_S1_RNA-bd_dom.
IPR019307. RNA-bd_AU-1/RNase_E/G.
IPR022967. RNA-binding_domain_S1.
IPR028878. RNase_E.
IPR004659. RNase_E/G.
[Graphical view ]
Pfami PF12111. PNPase_C. 1 hit.
PF10150. RNase_E_G. 1 hit.
PF00575. S1. 1 hit.
[Graphical view ]
SMARTi SM00316. S1. 1 hit.
[Graphical view ]
SUPFAMi SSF50249. SSF50249. 1 hit.
TIGRFAMsi TIGR00757. RNaseEG. 1 hit.
PROSITEi PS50126. S1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publicationsDownload
  1. "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
    Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.
    , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
    DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. "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.
  3. "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.
  4. "Cloning and analysis of the entire Escherichia coli ams gene. ams is identical to hmp1 and encodes a 114 kDa protein that migrates as a 180 kDa protein."
    Casaregola S., Jacq A., Laoudj D., McGurk G., Margarson S., Tempete M., Norris V., Holland I.B.
    J. Mol. Biol. 228:30-40(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1025.
    Strain: K12.
  5. "Analysis of the altered mRNA stability (ams) gene from Escherichia coli. Nucleotide sequence, transcriptional analysis, and homology of its product to MRP3, a mitochondrial ribosomal protein from Neurospora crassa."
    Claverie-Martin F., Diaz-Torres M., Yancey S.D., Kushner S.R.
    J. Biol. Chem. 266:2843-2851(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-844.
    Strain: K12.
  6. "Sequencing and expression of the rne gene of Escherichia coli."
    Chauhan A.K., Miczak A., Taraseviciene L., Apirion D.
    Nucleic Acids Res. 19:125-129(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-27.
    Strain: K12.
  7. "RNase E activity is conferred by a single polypeptide: overexpression, purification, and properties of the ams/rne/hmp1 gene product."
    Cormack R.S., Genereaux J.L., Mackie G.A.
    Proc. Natl. Acad. Sci. U.S.A. 90:9006-9010(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 844-1061, CHARACTERIZATION.
    Strain: K12.
  8. "Maturation of 5-S rRNA: ribonuclease E cleavages and their dependence on precursor sequences."
    Roy M.K., Singh B., Ray B.K., Apirion D.
    Eur. J. Biochem. 131:119-127(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN 5S RRNA MATURATION.
  9. "Escherichia coli cell division inhibitor DicF-RNA of the dicB operon. Evidence for its generation in vivo by transcription termination and by RNase III and RNase E-dependent processing."
    Faubladier M., Cam K., Bouche J.P.
    J. Mol. Biol. 212:461-471(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PROCESSING OF DICF-RNA.
  10. "RNase E, an endoribonuclease, has a general role in the chemical decay of Escherichia coli mRNA: evidence that rne and ams are the same genetic locus."
    Mudd E.A., Krisch H.M., Higgins C.F.
    Mol. Microbiol. 4:2127-2135(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Ribonuclease E organizes the protein interactions in the Escherichia coli RNA degradosome."
    Vanzo N.F., Li Y.S., Py B., Blum E., Higgins C.F., Raynal L.C., Krisch H.M., Carpousis A.J.
    Genes Dev. 12:2770-2781(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RHLB; PNPASE AND ENOLASE, DOMAIN.
  12. "RNase G (CafA protein) and RNase E are both required for the 5' maturation of 16S ribosomal RNA."
    Li Z., Pandit S., Deutscher M.P.
    EMBO J. 18:2878-2885(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN 16S RRNA MATURATION.
    Strain: K12.
  13. "RNA degradosomes exist in vivo in Escherichia coli as multicomponent complexes associated with the cytoplasmic membrane via the N-terminal region of ribonuclease E."
    Liou G.G., Jane W.N., Cohen S.N., Lin N.S., Lin-Chao S.
    Proc. Natl. Acad. Sci. U.S.A. 98:63-68(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
  14. "Cleavage of poly(A) tails on the 3'-end of RNA by ribonuclease E of Escherichia coli."
    Walsh A.P., Tock M.R., Mallen M.H., Kaberdin V.R., Gabain Av A., McDowall K.J.
    Nucleic Acids Res. 29:1864-1871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CLEAVAGE OF POLY(A).
  15. "RNase E plays an essential role in the maturation of Escherichia coli tRNA precursors."
    Li Z., Deutscher M.P.
    RNA 8:97-109(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRNA MATURATION.
    Strain: K12.
  16. "Physical and functional interactions among RNase E, polynucleotide phosphorylase and the cold-shock protein, CsdA: evidence for a 'cold shock degradosome'."
    Prud'homme-Genereux A., Beran R.K., Iost I., Ramey C.S., Mackie G.A., Simons R.W.
    Mol. Microbiol. 54:1409-1421(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DEAD.
    Strain: CF881.
  17. "'Zn-link': a metal-sharing interface that organizes the quaternary structure and catalytic site of the endoribonuclease, RNase E."
    Callaghan A.J., Redko Y., Murphy L.M., Grossmann J.G., Yates D., Garman E., Ilag L.L., Robinson C.V., Symmons M.F., McDowall K.J., Luisi B.F.
    Biochemistry 44:4667-4675(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, RNA-BINDING, SUBUNIT, ZINC-BINDING, COFACTOR, MASS SPECTROMETRY, MUTAGENESIS OF CYS-404 AND CYS-407.
  18. "RNaseE and RNA helicase B play central roles in the cytoskeletal organization of the RNA degradosome."
    Taghbalout A., Rothfield L.
    J. Biol. Chem. 283:13850-13855(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RHLB; PNPASE AND ENOLASE.
  19. "Rapid cleavage of RNA by RNase E in the absence of 5' monophosphate stimulation."
    Kime L., Jourdan S.S., Stead J.A., Hidalgo-Sastre A., McDowall K.J.
    Mol. Microbiol. 76:590-604(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF THR-170.
  20. "Membrane binding of Escherichia coli RNase E catalytic domain stabilizes protein structure and increases RNA substrate affinity."
    Murashko O.N., Kaberdin V.R., Lin-Chao S.
    Proc. Natl. Acad. Sci. U.S.A. 109:7019-7024(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, SUBCELLULAR LOCATION.
  21. "Structural characterization of the RNase E S1 domain and identification of its oligonucleotide-binding and dimerization interfaces."
    Schubert M., Edge R.E., Lario P., Cook M.A., Strynadka N.C., Mackie G.A., McIntosh L.P.
    J. Mol. Biol. 341:37-54(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 35-125, STRUCTURE BY NMR OF 35-125, SUBUNIT, RNA-BINDING, DOMAIN, MUTAGENESIS OF GLY-66.
  22. "Structure of Escherichia coli RNase E catalytic domain and implications for RNA turnover."
    Callaghan A.J., Marcaida M.J., Stead J.A., McDowall K.J., Scott W.G., Luisi B.F.
    Nature 437:1187-1191(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-510 IN COMPLEXES WITH RNA; ZINC AND MAGNESIUM IONS, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF PHE-57; PHE-67; LYS-112; THR-170; ASP-303; ASN-305; ASP-346 AND ARG-373.
  23. "Recognition of enolase in the Escherichia coli RNA degradosome."
    Chandran V., Luisi B.F.
    J. Mol. Biol. 358:8-15(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 833-850 IN COMPLEX WITH ENO, SUBUNIT.
  24. "The crystal structure of the Escherichia coli RNase E apoprotein and a mechanism for RNA degradation."
    Koslover D.J., Callaghan A.J., Marcaida M.J., Garman E.F., Martick M., Scott W.G., Luisi B.F.
    Structure 16:1238-1244(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-515 IN COMPLEX WITH RNA AND ZINC IONS, SUBUNIT.
  25. "Crystal structure of Escherichia coli polynucleotide phosphorylase core bound to RNase E, RNA and manganese: implications for catalytic mechanism and RNA degradosome assembly."
    Nurmohamed S., Vaidialingam B., Callaghan A.J., Luisi B.F.
    J. Mol. Biol. 389:17-33(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1021-1061 IN COMPLEXES WITH PNP AND RNA, SUBUNIT.
  26. "Molecular recognition between Escherichia coli enolase and ribonuclease E."
    Nurmohamed S., McKay A.R., Robinson C.V., Luisi B.F.
    Acta Crystallogr. D 66:1036-1040(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 823-850 IN COMPLEX WITH ENO, INTERACTION WITH ENO, MASS SPECTROMETRY, SUBUNIT.

Entry nameiRNE_ECOLI
AccessioniPrimary (citable) accession number: P21513
Secondary accession number(s): P77591
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: August 29, 2003
Last modified: March 19, 2014
This is version 141 of the entry and version 6 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

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