Escherichia coli K-12 substr. MG1655 Enzyme: enolase

Gene: eno Accession Numbers: EG10258 (EcoCyc), b2779, ECK2773

Regulation Summary Diagram: ?

Regulation summary diagram for eno

Component of: degradosome (extended summary available)

Subunit composition of enolase = [Eno]2

Enolase catalyzes the interconversion of 2-phosphoglycerate and phosphoenolpyruvate during glycolysis and gluconeogenesis in E. coli. It is also a component of the E. coli degradosome complex that degrades RNA. In the degradosome enolase has been shown to bind to the C-terminal scaffold region of ribonuclease E. However, the role of enolase in RNA metabolism has not been fully defined [Miczak96, Kuhnel01, Liou01, Morita04, Callaghan04, Chandran06, Nurmohamed10, DominguezMalfav13, Lu14].

Enolase has been purified from cell extracts of E. coli B and characterized. It was shown to be a dimer in solution and is dependent upon Mg2+ for its structure [Spring71]. The E. coli K-12 eno gene was later cloned, sequenced and functionally expressed in a temperature-sensitive eno mutant strain [Klein96].

The crystal structure of recombinant enolase from E. coli K-12 has been determined at 2.5 Å resolution, revealing that its dimer interface is enriched in charged residues relative to typical homodimer interfaces [Kuhnel01]. A later 1.6 Å structure shows enolase bound to its recognition site on RNase E [Chandran06].

E. coli enolase is functionally similar to enolases in other organisms, notably in its dependence on Mg2+, inhibition by fluoride in the presence of phosphate, and in its catalytic parameters. Its pH optimum is significantly higher than vertebrate enolases and is somewhat above those of yeast and plant enolases [Spring71].

E. coli K-12 enolase mutants were shown to grow on glycerate and succinate. They accumulated glycolytic pathway intermediates above the blocked enzyme upon addition of glucose or glycerol to resting cultures [Irani77].

Enolase is required for the rapid, degradosome-mediated degradation of ptsG mRNA in response to high levels of glucose 6-phosphate or fructose 6-phosphate [Morita04].

Immunofluorescence microscopy studies showed that enolase and other components of the degradosome are associated with the E. coli cytoskeleton and are organized into extended helical structures [Taghbalout07].

Reviews: [Gerlt05, Burger11]

Gene Citations: [Shimada05]

Locations: cytosol, extracellular space, cytoskeleton, membrane

Map Position: [2,904,665 <- 2,905,963] (62.6 centisomes, 225°)
Length: 1299 bp / 432 aa

Molecular Weight of Polypeptide: 45.655 kD (from nucleotide sequence), 46.0 kD (experimental) [Spring71 ]

Molecular Weight of Multimer: 90.0 kD (experimental) [Spring71]

pI: 5.64, 5.7

Unification Links: ASAP:ABE-0009110 , CGSC:823 , DIP:DIP-31847N , EchoBASE:EB0254 , EcoGene:EG10258 , EcoliWiki:b2779 , Mint:MINT-1230935 , ModBase:P0A6P9 , OU-Microarray:b2779 , PortEco:eno , PR:PRO_000022518 , Pride:P0A6P9 , Protein Model Portal:P0A6P9 , RefSeq:NP_417259 , RegulonDB:EG10258 , SMR:P0A6P9 , String:511145.b2779 , UniProt:P0A6P9

Relationship Links: InterPro:IN-FAMILY:IPR000941 , InterPro:IN-FAMILY:IPR020809 , InterPro:IN-FAMILY:IPR020810 , InterPro:IN-FAMILY:IPR020811 , InterPro:IN-FAMILY:IPR029017 , InterPro:IN-FAMILY:IPR029065 , Panther:IN-FAMILY:PTHR11902 , PDB:Structure:1E9I , PDB:Structure:2FYM , PDB:Structure:3H8A , Pfam:IN-FAMILY:PF00113 , Pfam:IN-FAMILY:PF03952 , Prints:IN-FAMILY:PR00148 , Prosite:IN-FAMILY:PS00164

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for eno

GO Terms:

Biological Process: GO:0006096 - glycolytic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, UniProtGOA11, GOA06, GOA01, Irani77]
Molecular Function: GO:0000287 - magnesium ion binding Inferred from experiment Inferred by computational analysis [GOA06, GOA01, Chandran06]
GO:0004634 - phosphopyruvate hydratase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, GOA01, Kuhnel01, Poyner02, Spring71]
GO:0005515 - protein binding Inferred from experiment [AitBara10, Chandran06, Regonesi06, Butland05, Callaghan04]
GO:0042802 - identical protein binding Inferred from experiment [Lasserre06, Callaghan04]
GO:0042803 - protein homodimerization activity Inferred from experiment [Kuhnel01]
GO:0016829 - lyase activity Inferred by computational analysis [UniProtGOA11]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, Zhang07a, LopezCampistrou05, Lasserre06]
GO:0005856 - cytoskeleton Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, Taghbalout07]
GO:0016020 - membrane Inferred from experiment [Lasserre06]
GO:0000015 - phosphopyruvate hydratase complex Inferred by computational analysis [GOA01]
GO:0005576 - extracellular region Inferred by computational analysis [UniProtGOA11a, UniProtGOA11]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, GOA06]
GO:0009986 - cell surface Inferred by computational analysis [UniProtGOA11a, GOA06]

MultiFun Terms: metabolism central intermediary metabolism
metabolism energy metabolism, carbon glycolysis

Essentiality data for eno knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Last-Curated ? 26-Feb-2015 by Fulcher C , SRI International

Enzymatic reaction of: enolase

Synonyms: phosphopyruvate hydratase, 2-phosphoglycerate dehydratase, 2,3-diphospho-D-glycerate, 2-phospho-D glycerate phosphotransferase, 2-phospho-D-glycerate hydrolyase

EC Number:

2-phospho-D-glycerate <=> phosphoenolpyruvate + H2O

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

This reaction is reversible. [Chandran06]

In Pathways: superpathway of hexitol degradation (bacteria) , superpathway of glycolysis and Entner-Doudoroff , superpathway of glycolysis, pyruvate dehydrogenase, TCA, and glyoxylate bypass , gluconeogenesis I , glycolysis II (from fructose 6-phosphate) , glycolysis I (from glucose 6-phosphate)

The data from [Spring71] are for the E. coli B enzyme. Fluoride inhibition occurs in the presence of phosphate. EDTA caused an irreversible loss of enolase activity, suggesting destabilization of the enzyme in the absence of Mg2+ [Spring71].

Cofactors or Prosthetic Groups: Mg2+ [Spring71]

Cofactor Binding Comment: Magnesium is required for catalysis and stabilizing the dimer. There is an absolute dependence on divalent cations for activity.[Spring71]

Inhibitors (Unknown Mechanism): fluoride [Spring71]

Kinetic Parameters:

Km (μM)

pH(opt): 8.1 [Spring71]

Subunit of: degradosome

Subunit composition of degradosome = [(Ppk)2][(Rne)4][(RhlB)2][(Pnp)3][(Eno)2]
         polyphosphate kinase = (Ppk)2 (extended summary available)
         ribonuclease E = (Rne)4 (extended summary available)
                 RNase E = Rne
         RhlB, ATP-dependent RNA helicase of the RNA degradosome = (RhlB)2 (extended summary available)
         polynucleotide phosphorylase = (Pnp)3 (extended summary available)
                 polynucleotide phosphorylase monomer = Pnp
         enolase = (Eno)2 (extended summary available)

The degradosome is a large, multiprotein complex involved in RNA degradation. It consists of the RNA degradation enzymes RNase E and PNPase, as well as the ATP-dependent RNA helicase RhlB and the metabolic enzyme enolase [Py94, Carpousis94, Py96]. Polyphosphate kinase and the chaperone protein DnaK are also associated with and may be components of the degradosome [Blum97, Miczak96]. A "minimal" degradosome composed of only RNase E, PNPase and RhlB degrades malEF REP RNA in an ATP-dependent manner in vitro, with activity equivalent to purified whole degradosomes. RNase E enzymatic function is dispensible for this test case, whereas PNPase must be catalytically active and incorporated into the degradosome for degradation to occur [Coburn99]. Based on immunogold labeling studies, RhlB and RNase E are present in equimolar quantities in the degradosome, which is tethered to the cytoplasmic membrane via the amino-terminus of RNase E [Liou01].

RNase E provides the organizational structure for the degradosome. Its carboxy-terminal half binds PNPase, RhlB and enolase, and the loss of this portion of the protein prevents degradation of a number of degradosome substrates, including the ptsG and mukB mRNAs and RNA I [Kido96, Vanzo98, Morita04]. This scaffold region is flexible, with isolated segments of increased structure that may be involved in binding other degradosome constituents [Callaghan04]. RNase E binding to partner proteins can be selectively disrupted. Loss of RhlB and enolase binding results in reduced degradosome activity. Conversely, disrupted PNPase binding yields increased activity. Strains any alteration in RNase E binding do not grow as well as wild type [Leroy02]. The amino-terminal half of RNase E contains sequences involved in oligomerization [Vanzo98].

In vitro purified degradosome generates 147-nucleotide RNase E cleavage intermediates from rpsT mRNA. Continuous cycles of polyadenylation and PNPase cleavage are necessary and sufficient to break down these intermediates, though RNase II can block this second degradation step [Coburn98]. RNAs with 3' REP stabilizers or stem loops must be polyadenylated to allow breakdown by the degradosome [Khemici04, Blum99]. Poly(G) and poly(U) tails do not allow degradation, though addition of a stretch of mixed nucleotides copied from within a coding region has stimulated degradation of a test substrate [Blum99].

The degradosome copurifies with fragments from its RNA substrates, including rRNA fragments derived from cleavage of 16S and 23S rRNA by RNase E, 5S rRNA and ssrA RNA [Bessarab98, LinChao99].

The DEAD-box helicases SrmB, RhlE and CsdA bind RNase E in vitro at a different site than RhlB. RhlE and CsdA can both replace RhlB in promoting PNPase activity in vitro [Khemici04a]. CsdA is induced by cold shock, and following a shift to 15 degrees C it copurifies with the degradosome [PrudhommeGenere04].

At least two poly(A)-binding proteins interact with the degradosome. The cold-shock protein CspE inhibits internal cleavage and breakdown of polyadenylated RNA by RNase E and PNPase by blocking digestion through the poly(A) tail. S1, a component of the 30S ribosome, binds to RNase E and PNPase without apparent effect on their activities [Feng01a].

The global effects of mutations in degradeosome constituents on mRNA levels have been evaluated using microarrays [Bernstein04].

Locations: inner membrane

GO Terms:

Cellular Component: GO:0005886 - plasma membrane [Liou01]

Sequence Features

Protein sequence of Eno with features indicated

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[Py96, Wilkins98, Link97, UniProt11]
UniProt: Removed.
Chain 2 -> 432
UniProt: Enolase;
Protein-Segment 5 -> 34
UniProt: Interaction with RNase E; Sequence Annotation Type: region of interest.
Acetylation-Modification 6
Sequence-Conflict 102
[Klein94, UniProt15]
UniProt: (in Ref. 1; CAA57795/AAA24486).
Amino-Acid-Site 120
UniProt: Interaction with RNase E; Sequence Annotation Type: site.
Amino-Acid-Sites-That-Bind 159
UniProt: Substrate; Non-Experimental Qualifier: by similarity;
Mutagenesis-Variant 168
[Boel04, UniProt11]
UniProt: 5% activity; not secreted.
Amino-Acid-Sites-That-Bind 168
UniProt: Substrate; Non-Experimental Qualifier: by similarity;
Mutagenesis-Variant 209
[Boel04, UniProt11]
UniProt: 1% activity; not secreted.
Active-Site 209
UniProt: Proton donor; Non-Experimental Qualifier: by similarity;
Sequence-Conflict 220
[Klein94, UniProt15]
UniProt: (in Ref. 1; CAA57795).
Metal-Binding-Site 246
UniProt: Magnesium.
N6-acetyllysine-Modification 257
[Zhang09, UniProt15]
UniProt: N6-acetyllysine.
Metal-Binding-Site 290
UniProt: Magnesium.
Metal-Binding-Site 317
UniProt: Magnesium.
Sequence-Conflict 339
[Klein94, UniProt15]
UniProt: (in Ref. 1; CAA57795).
Amino-Acid-Sites-That-Bind 342
UniProt: Substrate (covalent); in inhibited form.
Mutagenesis-Variant 342
[Boel04, UniProt11]
[Boel04, UniProt11]
K → A, Q or R: 1% activity; not secreted.
K → E: 94% activity; not secreted.
Acetylation-Modification 342
Active-Site 342
UniProt: Proton acceptor; Non-Experimental Qualifier: by similarity;
Protein-Segment 369 -> 372
UniProt: Substrate binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity;
Amino-Acid-Site 376
UniProt: Interaction with RNase E; Sequence Annotation Type: site.
Amino-Acid-Sites-That-Bind 393
UniProt: Substrate; Non-Experimental Qualifier: by similarity;
Amino-Acid-Site 408
UniProt: Interaction with RNase E; Sequence Annotation Type: site.
Sequence-Conflict 421 -> 432
[Klein94, UniProt15]
UniProt: (in Ref. 1; CAA57795).

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram


10/20/97 Gene b2779 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10258; confirmed by SwissProt match.


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Blum97: Blum E, Py B, Carpousis AJ, Higgins CF (1997). "Polyphosphate kinase is a component of the Escherichia coli RNA degradosome." Mol Microbiol 1997;26(2);387-98. PMID: 9383162

Blum99: Blum E, Carpousis AJ, Higgins CF (1999). "Polyadenylation promotes degradation of 3'-structured RNA by the Escherichia coli mRNA degradosome in vitro." J Biol Chem 274(7);4009-16. PMID: 9933592

Boel04: Boel G, Pichereau V, Mijakovic I, Maze A, Poncet S, Gillet S, Giard JC, Hartke A, Auffray Y, Deutscher J (2004). "Is 2-phosphoglycerate-dependent automodification of bacterial enolases implicated in their export?." J Mol Biol 337(2);485-96. PMID: 15003462

Burger11: Burger A, Whiteley C, Boshoff A (2011). "Current perspectives of the Escherichia coli RNA degradosome." Biotechnol Lett 33(12);2337-50. PMID: 21805185

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Callaghan04: Callaghan AJ, Aurikko JP, Ilag LL, Gunter Grossmann J, Chandran V, Kuhnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF (2004). "Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E." J Mol Biol 340(5);965-79. PMID: 15236960

Carpousis94: Carpousis AJ, Van Houwe G, Ehretsmann C, Krisch HM (1994). "Copurification of E. coli RNAase E and PNPase: evidence for a specific association between two enzymes important in RNA processing and degradation." Cell 76(5);889-900. PMID: 7510217

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Coburn98: Coburn GA, Mackie GA (1998). "Reconstitution of the degradation of the mRNA for ribosomal protein S20 with purified enzymes." J Mol Biol 279(5);1061-74. PMID: 9642084

Coburn99: Coburn GA, Miao X, Briant DJ, Mackie GA (1999). "Reconstitution of a minimal RNA degradosome demonstrates functional coordination between a 3' exonuclease and a DEAD-box RNA helicase." Genes Dev 13(19);2594-603. PMID: 10521403

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

DominguezMalfav13: Dominguez-Malfavon L, Islas LD, Luisi BF, Garcia-Villegas R, Garcia-Mena J (2013). "The assembly and distribution in vivo of the Escherichia coli RNA degradosome." Biochimie 95(11);2034-41. PMID: 23927922

Feng01a: Feng Y, Huang H, Liao J, Cohen SN (2001). "Escherichia coli poly(A)-binding proteins that interact with components of degradosomes or impede RNA decay mediated by polynucleotide phosphorylase and RNase E." J Biol Chem 276(34);31651-6. PMID: 11390393

Gerlt05: Gerlt JA, Babbitt PC, Rayment I (2005). "Divergent evolution in the enolase superfamily: the interplay of mechanism and specificity." Arch Biochem Biophys 433(1);59-70. PMID: 15581566

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Irani77: Irani MH, Maitra PK (1977). "Properties of Escherichia coli mutants deficient in enzymes of glycolysis." J Bacteriol 132(2);398-410. PMID: 410789

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Khemici04: Khemici V, Carpousis AJ (2004). "The RNA degradosome and poly(A) polymerase of Escherichia coli are required in vivo for the degradation of small mRNA decay intermediates containing REP-stabilizers." Mol Microbiol 51(3);777-90. PMID: 14731278

Khemici04a: Khemici V, Toesca I, Poljak L, Vanzo NF, Carpousis AJ (2004). "The RNase E of Escherichia coli has at least two binding sites for DEAD-box RNA helicases: functional replacement of RhlB by RhlE." Mol Microbiol 54(5);1422-30. PMID: 15554979

Kido96: Kido M, Yamanaka K, Mitani T, Niki H, Ogura T, Hiraga S (1996). "RNase E polypeptides lacking a carboxyl-terminal half suppress a mukB mutation in Escherichia coli." J Bacteriol 178(13);3917-25. PMID: 8682798

Klein94: Klein M., Freudl R. (1994). Data submission to EMBL/GenBank/DDBJ databases on 1994-10.

Klein96: Klein M, Sprenger GA, Freudl R (1996). "Cloning, nucleotide sequence, and functional expression of the Escherichia coli enolase (eno) gene in a temperature-sensitive eno mutant strain." DNA Seq 6(6);351-5. PMID: 8988374

Kuhnel01: Kuhnel K, Luisi BF (2001). "Crystal structure of the Escherichia coli RNA degradosome component enolase." J Mol Biol 313(3);583-92. PMID: 11676541

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

Leroy02: Leroy A, Vanzo NF, Sousa S, Dreyfus M, Carpousis AJ (2002). "Function in Escherichia coli of the non-catalytic part of RNase E: role in the degradation of ribosome-free mRNA." Mol Microbiol 45(5);1231-43. PMID: 12207692

LinChao99: Lin-Chao S, Wei CL, Lin YT (1999). "RNase E is required for the maturation of ssrA RNA and normal ssrA RNA peptide-tagging activity." Proc Natl Acad Sci U S A 96(22);12406-11. PMID: 10535935

Link97: Link AJ, Robison K, Church GM (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18(8);1259-313. PMID: 9298646

Liou01: Liou GG, Jane WN, Cohen SN, Lin NS, Lin-Chao S (2001). "RNA degradosomes exist in vivo in Escherichia coli as multicomponent complexes associated with the cytoplasmic membrane via the N-terminal region of ribonuclease E." Proc Natl Acad Sci U S A 98(1);63-8. PMID: 11134527

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Lu14: Lu F, Taghbalout A (2014). "The Escherichia coli major exoribonuclease RNase II is a component of the RNA degradosome." Biosci Rep 34(6);e00166. PMID: 25299745

Miczak96: Miczak A, Kaberdin VR, Wei CL, Lin-Chao S (1996). "Proteins associated with RNase E in a multicomponent ribonucleolytic complex." Proc Natl Acad Sci U S A 93(9);3865-9. PMID: 8632981

Morita04: Morita T, Kawamoto H, Mizota T, Inada T, Aiba H (2004). "Enolase in the RNA degradosome plays a crucial role in the rapid decay of glucose transporter mRNA in the response to phosphosugar stress in Escherichia coli." Mol Microbiol 54(4);1063-75. PMID: 15522087

Nurmohamed10: Nurmohamed S, McKay AR, Robinson CV, Luisi BF (2010). "Molecular recognition between Escherichia coli enolase and ribonuclease E." Acta Crystallogr D Biol Crystallogr 66(Pt 9);1036-40. PMID: 20823555

Poyner02: Poyner RR, Larsen TM, Wong SW, Reed GH (2002). "Functional and structural changes due to a serine to alanine mutation in the active-site flap of enolase." Arch Biochem Biophys 401(2);155-63. PMID: 12054465

PrudhommeGenere04: Prud'homme-Genereux A, Beran RK, Iost I, Ramey CS, Mackie GA, Simons RW (2004). "Physical and functional interactions among RNase E, polynucleotide phosphorylase and the cold-shock protein, CsdA: evidence for a 'cold shock degradosome'." Mol Microbiol 54(5);1409-21. PMID: 15554978

Py94: Py B, Causton H, Mudd EA, Higgins CF (1994). "A protein complex mediating mRNA degradation in Escherichia coli." Mol Microbiol 14(4);717-29. PMID: 7891559

Py96: Py B, Higgins CF, Krisch HM, Carpousis AJ (1996). "A DEAD-box RNA helicase in the Escherichia coli RNA degradosome." Nature 381(6578);169-72. PMID: 8610017

Regonesi06: Regonesi ME, Del Favero M, Basilico F, Briani F, Benazzi L, Tortora P, Mauri P, Deho G (2006). "Analysis of the Escherichia coli RNA degradosome composition by a proteomic approach." Biochimie 88(2);151-61. PMID: 16139413

Shimada05: Shimada T, Fujita N, Maeda M, Ishihama A (2005). "Systematic search for the Cra-binding promoters using genomic SELEX system." Genes Cells 10(9);907-18. PMID: 16115199

Spring71: Spring TG, Wold F (1971). "The purification and characterization of Escherichia coli enolase." J Biol Chem 1971;246(22);6797-802. PMID: 4942326

Taghbalout07: Taghbalout A, Rothfield L (2007). "RNaseE and the other constituents of the RNA degradosome are components of the bacterial cytoskeleton." Proc Natl Acad Sci U S A 104(5);1667-72. PMID: 17242352

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProt14: UniProt Consortium (2014). "UniProt version 2014-01 released on 2014-01-01 00:00:00." Database.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Vanzo98: Vanzo NF, Li YS, Py B, Blum E, Higgins CF, Raynal LC, Krisch HM, Carpousis AJ (1998). "Ribonuclease E organizes the protein interactions in the Escherichia coli RNA degradosome." Genes Dev 12(17);2770-81. PMID: 9732274

Wilkins98: Wilkins MR, Gasteiger E, Tonella L, Ou K, Tyler M, Sanchez JC, Gooley AA, Walsh BJ, Bairoch A, Appel RD, Williams KL, Hochstrasser DF (1998). "Protein identification with N and C-terminal sequence tags in proteome projects." J Mol Biol 278(3);599-608. PMID: 9600841

Yu08: Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG (2008). "The diversity of lysine-acetylated proteins in Escherichia coli." J Microbiol Biotechnol 18(9);1529-36. PMID: 18852508

Zhang07a: Zhang N, Chen R, Young N, Wishart D, Winter P, Weiner JH, Li L (2007). "Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS." Proteomics 7(4);484-93. PMID: 17309111

Zhang09: Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8(2);215-25. PMID: 18723842

Other References Related to Gene Regulation

MendozaVargas09: Mendoza-Vargas A, Olvera L, Olvera M, Grande R, Vega-Alvarado L, Taboada B, Jimenez-Jacinto V, Salgado H, Juarez K, Contreras-Moreira B, Huerta AM, Collado-Vides J, Morett E (2009). "Genome-wide identification of transcription start sites, promoters and transcription factor binding sites in E. coli." PLoS One 4(10);e7526. PMID: 19838305

Olvera09: Olvera L, Mendoza-Vargas A, Flores N, Olvera M, Sigala JC, Gosset G, Morett E, Bolivar F (2009). "Transcription analysis of central metabolism genes in Escherichia coli. Possible roles of sigma38 in their expression, as a response to carbon limitation." PLoS One 4(10);e7466. PMID: 19838295

Weng86: Weng M, Makaroff CA, Zalkin H (1986). "Nucleotide sequence of Escherichia coli pyrG encoding CTP synthetase." J Biol Chem 1986;261(12);5568-74. PMID: 3514618

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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