Escherichia coli K-12 substr. MG1655 Protein: GTPase, involved in modification of U34 in tRNA

Gene: mnmE Accession Numbers: EG10997 (EcoCyc), b3706, ECK3699

Synonyms: trmE, thdF

Regulation Summary Diagram: ?

Regulation summary diagram for mnmE

Component of: 5-carboxymethylaminomethyluridine-tRNA synthase [multifunctional] (summary available)

Subunit composition of GTPase, involved in modification of U34 in tRNA = [MnmE]2
         GTPase, involved in modification of U34 in tRNA = MnmE

MnmE is required for wild-type 5-methylaminomethyl-2-thiouridine modification of tRNA [Elseviers84]. The additional modification of m5U stabilizes the U·G pairing at the wobble position and thus plays a role in decoding NNG codons [Kurata08].

Together with MnmG, MnmE is involved in maintenance of the correct reading frame [Brierley97, Urbonavicius01, Bregeon01, Urbonavicius03]. MnmE also appeared to play a role in oxidation of thiophene and furan compounds [Alam91] and regulates glutamate-dependent acid resistance [Gong04, Sayed09].

MnmE is a GTP-binding protein that also exhibits GTPase activity, showing rapid GTP hydrolysis and low nucleotide affinity. The nucleotide binding and hydrolysis activities are localized within the central 17 kDa GTPase domain [Cabedo99]. The GTPase activity as well as the Cys451 residue in the C-terminal domain are required for the wild-type tRNA modification function [Yim03], but not sufficient [MartinezVicente05]. Dimerization of the GTPase domain is potassium ion-dependent; subsequent GTP hydrolysis activity is dependent on dimerization [Scrima06]. Low pH inhibits the GTP hydrolysis activity [Monleon07]. Unlike other GTPases, MnmE does not appear to use an "arginine finger" for catalysis [Scrima06, Monleon07].

While the GTPase domain is required for homodimerization, the helical domain of MnmE is responsible for the interaction with MnmG [Meyer08a]. Nucleotide binding leads to a conformational change in MnmE, and GTP-bound MnmE has a much higher affinity for MnmG [Meyer09]. Conversely, MnmG binding induces large conformational changes in MnmE [Bohme10]. MnmG stabilizes the MnmE homodimer and stimulates GTP hydrolysis [Meyer09, Bohme10].

Solution and crystal structures of the G-domain of MnmE have been solved [Monleon04, Scrima06, Monleon07]. MnmE can homomultimerize and localizes to the cytoplasm, showing some association with the cytoplasmic membrane [Cabedo99]. MnmE interacts specifically with MnmG [Yim06]. A fraction of MnmE protein appears to be associated with the plasma membrane [Cabedo99].

Viability of an mnmE mutation is dependent on the strain background [Cabedo99]. mnmE mutants are defective in the tRNA modification 5-methylaminomethyl-2-thiouridine; tRNA anticodons that are modified with 5-methylaminomethyl-2-thiouridine in the wild type show 2-thiouridine modification in the mutant, and mutants exhibit a defect in UAG readthrough [Elseviers84]. Unexpectedly, the hypomodified tRNALys of an mnmE mutant leads to decreased misreading of the anticodon [Hagervall98]. An mnmE deletion enhances the slow growth phenotype of a ΔyjeQ mutant [Campbell08] and partially supresses the cold-sensitive growth phenotype and MiaB activity defect of a ygfZ null mutant [Waller12].

Expression of mnmE is increased during stationary phase, but independent of the stationary phase sigma factor RpoS. Expression is also subject to catabolite repression and is decreased in the absence of oxygen [Zabel00].

ThdF: "thiophene degradation" [Alam91]

TrmE: "tRNA modification" [Elseviers84]

MnmE: "methylaminomethyl modification"

Reviews: [Mittenhuber01, Caldon01, Verstraeten11, Armengod12, El12]

Citations: [Scrima05, Gruian12, Ash12, Deng13]

Locations: inner membrane, cytosol

Map Position: [3,884,851 -> 3,886,215] (83.73 centisomes, 301°)
Length: 1365 bp / 454 aa

Molecular Weight of Polypeptide: 49.231 kD (from nucleotide sequence), 48 kD (experimental) [Alam91 ], 50 kD (experimental)

Unification Links: ASAP:ABE-0012123 , CGSC:17806 , DIP:DIP-11033N , EchoBASE:EB0990 , EcoGene:EG10997 , EcoliWiki:b3706 , ModBase:P25522 , OU-Microarray:b3706 , PortEco:mnmE , PR:PRO_000023256 , Pride:P25522 , Protein Model Portal:P25522 , RefSeq:NP_418162 , RegulonDB:EG10997 , SMR:P25522 , String:511145.b3706 , UniProt:P25522

Relationship Links: InterPro:IN-FAMILY:IPR004520 , InterPro:IN-FAMILY:IPR005225 , InterPro:IN-FAMILY:IPR006073 , InterPro:IN-FAMILY:IPR018948 , InterPro:IN-FAMILY:IPR025867 , InterPro:IN-FAMILY:IPR027266 , InterPro:IN-FAMILY:IPR027368 , InterPro:IN-FAMILY:IPR027417 , PDB:Structure:1RFL , PDB:Structure:2GJ8 , PDB:Structure:2GJ9 , PDB:Structure:2GJA , Pfam:IN-FAMILY:PF01926 , Pfam:IN-FAMILY:PF10396 , Pfam:IN-FAMILY:PF12631 , Prosite:IN-FAMILY:PS51709

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0002098 - tRNA wobble uridine modification Inferred from experiment [Elseviers84, Moukadiri09]
GO:0006805 - xenobiotic metabolic process Inferred from experiment [Alam91]
GO:0009268 - response to pH Inferred from experiment [Gong04]
GO:0030488 - tRNA methylation Inferred from experiment [Elseviers84]
GO:0061077 - chaperone-mediated protein folding Inferred from experiment [Wang12e]
GO:0006400 - tRNA modification Inferred by computational analysis [GOA06, GOA01]
GO:0008033 - tRNA processing Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0003924 - GTPase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, Yim03]
GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Butland05]
GO:0005525 - GTP binding Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA06, GOA01, Cabedo99]
GO:0019003 - GDP binding Inferred from experiment [Scrima05]
GO:0030955 - potassium ion binding Inferred from experiment [Scrima06]
GO:0042803 - protein homodimerization activity Inferred from experiment [Meyer09]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005737 - cytoplasm Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06, Cabedo99]
GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Zhang07, Cabedo99, Watt07]
GO:0005886 - plasma membrane Inferred from experiment [Cabedo99]
GO:0005622 - intracellular Inferred by computational analysis [GOA01]

MultiFun Terms: information transfer RNA related RNA modification
information transfer RNA related tRNA

Essentiality data for mnmE knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]

Created 15-Jun-2007 by Keseler I , SRI International
Last-Curated ? 22-Jul-2013 by Keseler I , SRI International

Subunit of: 5-carboxymethylaminomethyluridine-tRNA synthase [multifunctional]

Subunit composition of 5-carboxymethylaminomethyluridine-tRNA synthase [multifunctional] = [(MnmE)2][(MnmG)2]
         GTPase, involved in modification of U34 in tRNA = (MnmE)2
                 GTPase, involved in modification of U34 in tRNA = MnmE
         protein involved in modification of U34 in tRNA = (MnmG)2
                 protein involved in modification of U34 in tRNA = MnmG

The heterotetrameric MnmEG complex is required for 5-carboxymethylaminomethyl modification of the wobble base of certain tRNAs. Both complex formation and GTP hydrolysis are required for tRNA modification activity [Meyer09, Moukadiri09].

Utilizing either ammonium or glycine as a substrate, the MnmEG complex catalyzes formation of the 5-aminomethyl- or 5-carboxymethylaminomethyl modification of tRNA at the U34 wobble base [Moukadiri09]. All its tRNA substrates can be modified via the ammonium pathway; growth conditions influence which modification pathway is utilized [Moukadiri14].

Thiolation of the C2 position (catalyzed by MnmA) and modification of the C5 position of U34 are independent of each other.

Citations: [Meyer08a, Yim06]

Created 15-Jun-2007 by Keseler I , SRI International
Last-Curated ? 16-Dec-2013 by Keseler I , SRI International

Enzymatic reaction of: 5-carboxymethylaminomethyluridine-tRNA synthase

a uridine34 in tRNA + GTP + a 5,10-methylene-tetrahydrofolate + glycine + H2O <=> a 5-carboxymethylaminomethyluridine in tRNA + GDP + a 7,8-dihydrofolate + phosphate

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.

Reversibility of this reaction is unspecified.

a 2-thiouridine34 in tRNA + GTP + glycine + a 5,10-methylene-tetrahydrofolate + H2O <=> a 5-carboxymethylaminomethyl-2-thiouridine in tRNA + GDP + a 7,8-dihydrofolate + phosphate

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.

Reversibility of this reaction is unspecified.

Cofactors or Prosthetic Groups: FAD [Moukadiri09]

Enzymatic reaction of: 5-aminomethyluridine-tRNA synthase

a 2-thiouridine34 in tRNA + a 5,10-methylene-tetrahydrofolate + ammonium + GTP + H2O <=> a 5-aminomethyl-2-thiouridine in tRNA + a 7,8-dihydrofolate + GDP + phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

Cofactors or Prosthetic Groups: FAD [Moukadiri09]

Kinetic Parameters:

Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
a 2-thiouridine34 in tRNA

Sequence Features

Protein sequence of GTPase, involved in modification of U34 in tRNA with features indicated

Feature Class Location Attached Group Citations Comment
Amino-Acid-Sites-That-Bind 23  
UniProt: Formyltetrahydrofolate; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 80  
UniProt: Formyltetrahydrofolate; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 120  
UniProt: Formyltetrahydrofolate; Non-Experimental Qualifier: by similarity;
Conserved-Region 216 -> 377  
UniProt: TrmE-type G.
Mutagenesis-Variant 224  
[MartinezVicente05, UniProt11]
UniProt: 1.5-fold decrease in GTPase activity and almost no change in affinity.
Metal-Binding-Site 226  
UniProt: Potassium.
Nucleotide-Phosphate-Binding-Region 226 -> 231 GTP
UniProt: GTP.
Mutagenesis-Variant 226  
[Scrima06, UniProt11]
[Scrima06, UniProt11]
N → A: 100-fold decrease in GTPase activity. 5-fold decrease of affinity for GTP.
N → K: 70-fold decrease in GTPase activity. 2-fold decrease of affinity for GTP.
Mutagenesis-Variant 228  
[Yim03, UniProt11]
UniProt: Loss of GTP binding and hydrolase activity. Completely impairs tRNA modifying function.
Metal-Binding-Site 230  
UniProt: Magnesium.
Metal-Binding-Site 245  
UniProt: Potassium; via carbonyl oxygen.
Nucleotide-Phosphate-Binding-Region 245 -> 251 GTP
UniProt: GTP.
Metal-Binding-Site 247  
UniProt: Potassium; via carbonyl oxygen.
Mutagenesis-Variant 249  
[MartinezVicente05, UniProt11]
UniProt: 22-fold decrease in GTPase activity and 7-fold increase of affinity.
Metal-Binding-Site 250  
UniProt: Potassium.
Mutagenesis-Variant 250  
[MartinezVicente05, UniProt11]
[MartinezVicente05, UniProt11]
T → S: 1.8-fold decrease in GTPase activity and 1.5-fold increase of affinity.
T → A: 4-fold decrease in GTPase activity and 1.5-fold increase of affinity.
Metal-Binding-Site 251  
UniProt: Magnesium.
Mutagenesis-Variant 251  
[MartinezVicente05, UniProt11]
[MartinezVicente05, UniProt11]
T → S: 4-fold decrease in GTPase activity and 1.2-fold decrease of affinity.
T → A: 92-fold decrease in GTPase activity and 59-fold increase of affinity.
Mutagenesis-Variant 252  
[MartinezVicente05, UniProt11]
[MartinezVicente05, UniProt11]
R → K: 2-fold decrease in GTPase activity and no change in affinity.
R → A: 7-fold decrease in GTPase activity and 6-fold increase of affinity.
Mutagenesis-Variant 253  
[MartinezVicente05, UniProt11]
UniProt: 9-fold decrease in GTPase activity and 13-fold increase of affinity.
Mutagenesis-Variant 255  
[Scrima06, UniProt11]
UniProt: 1.5-fold decrease in affinity for GTP.
Mutagenesis-Variant 256  
[MartinezVicente05, UniProt11]
UniProt: 2-fold decrease in GTPase activity and almost no change in affinity.
Nucleotide-Phosphate-Binding-Region 270 -> 273 GTP
UniProt: GTP.
Mutagenesis-Variant 270  
[Yim03, UniProt11]
UniProt: Does not affect GTP binding, but impairs hydrolase activity. Completely impairs tRNA modifying function.
Mutagenesis-Variant 275  
[MartinezVicente05, UniProt11]
UniProt: 6-fold decrease in GTPase activity and 1.9-fold increase of affinity.
Mutagenesis-Variant 282  
[Scrima06, UniProt11]
[Scrima06, UniProt11]
E → A: 1900-fold decrease in GTPase activity.
E → Q: 370-fold decrease in GTPase activity.
Mutagenesis-Variant 288  
[MartinezVicente05, UniProt11]
UniProt: 1.7-fold decrease in GTPase activity and 1.5-fold increase of affinity.
Nucleotide-Phosphate-Binding-Region 335 -> 338 GTP
UniProt: GTP.
Mutagenesis-Variant 338  
[Yim03, UniProt11]
UniProt: Strong decrease in GTP binding. Does not affect hydrolase activity, but has 10-fold higher affinity for XTP than for GTP. Partially impairs tRNA modifying function.
Nucleotide-Phosphate-Binding-Region 358 -> 360 GTP
UniProt: GTP.
Mutagenesis-Variant 451  
[Yim03, UniProt11]
UniProt: No change in GTP binding and hydrolase activity. Does not affect association to the cell inner membrane. Completely impairs tRNA modifying function.
Amino-Acid-Sites-That-Bind 454  
UniProt: Formyltetrahydrofolate; Non-Experimental Qualifier: by similarity;

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


10/20/97 Gene b3706 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10997; confirmed by SwissProt match.


Alam91: Alam KY, Clark DP (1991). "Molecular cloning and sequence of the thdF gene, which is involved in thiophene and furan oxidation by Escherichia coli." J Bacteriol 173(19);6018-24. PMID: 1917835

Armengod12: Armengod ME, Moukadiri I, Prado S, Ruiz-Partida R, Benitez-Paez A, Villarroya M, Lomas R, Garzon MJ, Martinez-Zamora A, Meseguer S, Navarro-Gonzalez C (2012). "Enzymology of tRNA modification in the bacterial MnmEG pathway." Biochimie 94(7);1510-20. PMID: 22386868

Ash12: Ash MR, Maher MJ, Mitchell Guss J, Jormakka M (2012). "The cation-dependent G-proteins: In a class of their own." FEBS Lett 586(16);2218-24. PMID: 22750478

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bohme10: Bohme S, Meyer S, Kruger A, Steinhoff HJ, Wittinghofer A, Klare JP (2010). "Stabilization of G domain conformations in the tRNA-modifying MnmE-GidA complex observed with double electron electron resonance spectroscopy." J Biol Chem 285(22);16991-7000. PMID: 20353943

Bregeon01: Bregeon D, Colot V, Radman M, Taddei F (2001). "Translational misreading: a tRNA modification counteracts a +2 ribosomal frameshift." Genes Dev 15(17);2295-306. PMID: 11544186

Brierley97: Brierley I, Meredith MR, Bloys AJ, Hagervall TG (1997). "Expression of a coronavirus ribosomal frameshift signal in Escherichia coli: influence of tRNA anticodon modification on frameshifting." J Mol Biol 270(3);360-73. PMID: 9237903

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

Cabedo99: Cabedo H, Macian F, Villarroya M, Escudero JC, Martinez-Vicente M, Knecht E, Armengod ME (1999). "The Escherichia coli trmE (mnmE) gene, involved in tRNA modification, codes for an evolutionarily conserved GTPase with unusual biochemical properties." EMBO J 18(24);7063-76. PMID: 10601028

Caldon01: Caldon CE, Yoong P, March PE (2001). "Evolution of a molecular switch: universal bacterial GTPases regulate ribosome function." Mol Microbiol 41(2);289-97. PMID: 11489118

Campbell08: Campbell TL, Brown ED (2008). "Genetic interaction screens with ordered overexpression and deletion clonesets implicate the Escherichia coli GTPase YjeQ in late ribosome biogenesis." J Bacteriol 190(7);2537-45. PMID: 18223068

Deng13: Deng Z, Shan Y, Pan Q, Gao X, Yan A (2013). "Anaerobic expression of the gadE-mdtEF multidrug efflux operon is primarily regulated by the two-component system ArcBA through antagonizing the H-NS mediated repression." Front Microbiol 4;194. PMID: 23874328

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

El12: El Yacoubi B, Bailly M, de Crecy-Lagard V (2012). "Biosynthesis and function of posttranscriptional modifications of transfer RNAs." Annu Rev Genet 46;69-95. PMID: 22905870

Elseviers84: Elseviers D, Petrullo LA, Gallagher PJ (1984). "Novel E. coli mutants deficient in biosynthesis of 5-methylaminomethyl-2-thiouridine." Nucleic Acids Res 12(8);3521-34. PMID: 6427754

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

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

Gong04: Gong S, Ma Z, Foster JW (2004). "The Era-like GTPase TrmE conditionally activates gadE and glutamate-dependent acid resistance in Escherichia coli." Mol Microbiol 54(4);948-61. PMID: 15522079

Gruian12: Gruian C, Vanea E, Simon S, Simon V (2012). "FTIR and XPS studies of protein adsorption onto functionalized bioactive glass." Biochim Biophys Acta 1824(7);873-81. PMID: 22575087

Hagervall98: Hagervall TG, Pomerantz SC, McCloskey JA (1998). "Reduced misreading of asparagine codons by Escherichia coli tRNALys with hypomodified derivatives of 5-methylaminomethyl-2-thiouridine in the wobble position." J Mol Biol 284(1);33-42. PMID: 9811540

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kurata08: Kurata S, Weixlbaumer A, Ohtsuki T, Shimazaki T, Wada T, Kirino Y, Takai K, Watanabe K, Ramakrishnan V, Suzuki T (2008). "Modified uridines with C5-methylene substituents at the first position of the tRNA anticodon stabilize U.G wobble pairing during decoding." J Biol Chem 283(27);18801-11. PMID: 18456657

MartinezVicente05: Martinez-Vicente M, Yim L, Villarroya M, Mellado M, Perez-Paya E, Bjork GR, Armengod ME (2005). "Effects of mutagenesis in the switch I region and conserved arginines of Escherichia coli MnmE protein, a GTPase involved in tRNA modification." J Biol Chem 280(35);30660-70. PMID: 15983041

Meyer08a: Meyer S, Scrima A, Versees W, Wittinghofer A (2008). "Crystal structures of the conserved tRNA-modifying enzyme GidA: implications for its interaction with MnmE and substrate." J Mol Biol 380(3);532-47. PMID: 18565343

Meyer09: Meyer S, Wittinghofer A, Versees W (2009). "G-domain dimerization orchestrates the tRNA wobble modification reaction in the MnmE/GidA complex." J Mol Biol 392(4);910-22. PMID: 19591841

Mittenhuber01: Mittenhuber G (2001). "Comparative genomics of prokaryotic GTP-binding proteins (the Era, Obg, EngA, ThdF (TrmE), YchF and YihA families) and their relationship to eukaryotic GTP-binding proteins (the DRG, ARF, RAB, RAN, RAS and RHO families)." J Mol Microbiol Biotechnol 2001;3(1);21-35. PMID: 11200227

Monleon04: Monleon D, Yim L, Martinez-Vicente M, Armengod ME, Celda B (2004). "Backbone 1H, 13C and 15N resonance assignments for the 18.7 kDa GTPase domain of Escherichia coli MnmE protein." J Biomol NMR 28(3);307-8. PMID: 14752268

Monleon07: Monleon D, Martinez-Vicente M, Esteve V, Yim L, Prado S, Armengod ME, Celda B (2007). "Structural insights into the GTPase domain of Escherichia coli MnmE protein." Proteins 66(3);726-39. PMID: 17143896

Moukadiri09: Moukadiri I, Prado S, Piera J, Velazquez-Campoy A, Bjork GR, Armengod ME (2009). "Evolutionarily conserved proteins MnmE and GidA catalyze the formation of two methyluridine derivatives at tRNA wobble positions." Nucleic Acids Res 37(21);7177-93. PMID: 19767610

Moukadiri14: Moukadiri I, Garzon MJ, Bjork GR, Armengod ME (2014). "The output of the tRNA modification pathways controlled by the Escherichia coli MnmEG and MnmC enzymes depends on the growth conditions and the tRNA species." Nucleic Acids Res 42(4);2602-23. PMID: 24293650

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Sayed09: Sayed AK, Foster JW (2009). "A 750 bp sensory integration region directs global control of the Escherichia coli GadE acid resistance regulator." Mol Microbiol 71(6);1435-50. PMID: 19220752

Scrima05: Scrima A, Vetter IR, Armengod ME, Wittinghofer A (2005). "The structure of the TrmE GTP-binding protein and its implications for tRNA modification." EMBO J 24(1);23-33. PMID: 15616586

Scrima06: Scrima A, Wittinghofer A (2006). "Dimerisation-dependent GTPase reaction of MnmE: how potassium acts as GTPase-activating element." EMBO J 25(12);2940-51. PMID: 16763562

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 2014-08 released on 2014-08-01 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."

Urbonavicius01: Urbonavicius J, Qian Q, Durand JM, Hagervall TG, Bjork GR (2001). "Improvement of reading frame maintenance is a common function for several tRNA modifications." EMBO J 20(17);4863-73. PMID: 11532950

Urbonavicius03: Urbonavicius J, Stahl G, Durand JM, Ben Salem SN, Qian Q, Farabaugh PJ, Bjork GR (2003). "Transfer RNA modifications that alter +1 frameshifting in general fail to affect -1 frameshifting." RNA 9(6);760-8. PMID: 12756333

Verstraeten11: Verstraeten N, Fauvart M, Versees W, Michiels J (2011). "The universally conserved prokaryotic GTPases." Microbiol Mol Biol Rev 75(3);507-42, second and third pages of table of contents. PMID: 21885683

Waller12: Waller JC, Ellens KW, Hasnain G, Alvarez S, Rocca JR, Hanson AD (2012). "Evidence that the Folate-Dependent Proteins YgfZ and MnmEG Have Opposing Effects on Growth and on Activity of the Iron-Sulfur Enzyme MiaB." J Bacteriol 194(2);362-7. PMID: 22081392

Wang12e: Wang X, Xue J, Sun Z, Qin Y, Gong W (2012). "Study on the chaperone properties of conserved GTPases." Protein Cell 3(1);44-50. PMID: 22246579

Watt07: Watt RM, Wang J, Leong M, Kung HF, Cheah KS, Liu D, Danchin A, Huang JD (2007). "Visualizing the proteome of Escherichia coli: an efficient and versatile method for labeling chromosomal coding DNA sequences (CDSs) with fluorescent protein genes." Nucleic Acids Res 35(6);e37. PMID: 17272300

Yim03: Yim L, Martinez-Vicente M, Villarroya M, Aguado C, Knecht E, Armengod ME (2003). "The GTPase activity and C-terminal cysteine of the Escherichia coli MnmE protein are essential for its tRNA modifying function." J Biol Chem 278(31);28378-87. PMID: 12730230

Yim06: Yim L, Moukadiri I, Bjork GR, Armengod ME (2006). "Further insights into the tRNA modification process controlled by proteins MnmE and GidA of Escherichia coli." Nucleic Acids Res 34(20);5892-905. PMID: 17062623

Zabel00: Zabel MD, Bunch PK, Clark DP (2000). "Regulation of the thdF gene, which is involved in thiophene oxidation by Escherichia coli K-12." Microbios 101(399);89-103. PMID: 10738982

Zhang07: 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

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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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