Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015 (Sat)
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015 (Sat)
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015 (Sat)
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015 (Sat)
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015 (Sat)

Escherichia coli K-12 substr. MG1655 Polypeptide: protein chain elongation factor EF-Ts

Gene: tsf Accession Numbers: EG11033 (EcoCyc), b0170, ECK0169

Synonyms: EF1B

Regulation Summary Diagram: ?

Regulation summary diagram for tsf

EF-Ts is an elongation factor associated with the ribosome; it functions as the guanine nucleotide exchange factor for the EF-Tu GTPase. EF-Ts was first identified in the "T" (for transfer) fraction consisting of a stable (Ts) and an unstable (Tu) component [LucasLenard66]. Two molecules each of elongation factor Ts and elongation factor Tu assemble into a complex [Miller69, Wittinghofer83, Kawashima96]. EF-Ts is essential for growth [Hwang89a, Baba06].

EF-Ts interacts with aminoacyl-tRNA-bound EF-Tu and regulates its affinity for GTP and aa-tRNA ligands. EF-Ts may regulate the stability of the EF-Tu-GTP-aa-tRNA ternary complex by facilitating the conformational changes within EF-Tu that are responsible for binding and release of aa-tRNAs [Burnett13].

EF-Ts enhances the rate of dissociation of GDP from EF-Tu within the EF-Tu-GDP-EF-Ts complex [Chau81, Wittinghofer83] by a factor of 6x104 [Gromadski02]. EF-Ts dissociates from the ternary EF-Tu-GDP/GTP-EF-Ts complex 103-104 times faster than from the binary EF-Tu-EF-Ts complex. Under conditions resembling those in vivo, the overall nucleotide exchange rate catalyzed by EF-Ts is 30 s-1 [Gromadski02]. The kinetics of the nucleotide exchange reaction has also been modelled [Manchester04].

A crystal structure of the EF-Tu-EF-Ts complex (EF-T) has been solved at 2.5 Å resolution. It shows two subunits each of EF-Ts and EF-Tu, where a coiled-coil motif of EF-Ts appears to be primarily responsible for dimerization [Kawashima96]. An EF-Ts mutant lacking this coiled-coil motif shows near-normal growth, but forms unstable EF-Tu-EF-Ts complexes in the presence of guanine nucleotides [Karring03].

The N-terminal part of EF-Ts is required for the nucleotide exchange activity [Bogestrand95] and appears to determine the strength of the interaction with EF-Tu [Zhang97c]. A conformational change in the N terminus may be essential for binding EF-Tu [Hwang97]. Further site-directed mutagenesis showed that residues within the N-terminal domain and subdomain C are important for interaction with EF-Tu [Zhang98b]. Residues that are thought to be involved in the guanine nucleotide exchange reaction have been mutagenized. The D80 and F81 residues are important, but not essential for activity; they appear to affect the interaction with EF-Tu [Zhang96f].

The mechanism of nucleotide exchange has been investigated. Initial contact of the N-terminal domain of EF-Ts with helix D of EF-Tu appears to weaken interactions with the guanine base; contacts with the phosphate binding site, promoting release of the phosphate moiety, take place later [Wieden02].

EF-Ts enhances phosphorylation of EF-Tu [Alexander95] and can act as a "steric chaperone" for EF-Tu mutants which do not fold correctly [Krab01].

In addition to its function as a translation elongation factor, EF-Ts is a host-supplied component of the phage Qβ RNA replicase complex [Blumenthal72, Blumenthal76]. An EF-Ts mutant that forms unstable EF-Tu-EF-Ts complexes is unable to form an active Qβ-polymerase complex; EF-Ts may thus be required to stably trap EF-Tu within the Qβ-polymerase [Karring04]. Crystal structures of the Qβ replicase core complex have been solved [Kidmose10, Takeshita10].

Reviews: [LucasLenard71, Andersen03]

Citations: [Han07, Wieden10, Pan11, Miyajima78]

Gene Citations: [An81]

Locations: cytosol, membrane

Map Position: [190,857 -> 191,708] (4.11 centisomes, 15°)
Length: 852 bp / 283 aa

Molecular Weight of Polypeptide: 30.423 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0000579 , CGSC:64 , DIP:DIP-31835N , EchoBASE:EB1026 , EcoGene:EG11033 , EcoliWiki:b0170 , Mint:MINT-1273899 , OU-Microarray:b0170 , PortEco:tsf , PR:PRO_000024132 , Pride:P0A6P1 , Protein Model Portal:P0A6P1 , RefSeq:NP_414712 , RegulonDB:EG11033 , SMR:P0A6P1 , String:511145.b0170 , UniProt:P0A6P1

Relationship Links: InterPro:IN-FAMILY:IPR000449 , InterPro:IN-FAMILY:IPR001816 , InterPro:IN-FAMILY:IPR009060 , InterPro:IN-FAMILY:IPR014039 , InterPro:IN-FAMILY:IPR018101 , Panther:IN-FAMILY:PTHR11741 , PDB:Structure:1EFU , PDB:Structure:3MMP , PDB:Structure:4Q7J , Pfam:IN-FAMILY:PF00627 , Pfam:IN-FAMILY:PF00889 , Prosite:IN-FAMILY:PS01126 , Prosite:IN-FAMILY:PS01127

Genetic Regulation Schematic: ?

Genetic regulation schematic for tsf

GO Terms:

Biological Process: GO:0043547 - positive regulation of GTPase activity Inferred from experiment [Gromadski02]
GO:0006412 - translation Inferred by computational analysis [UniProtGOA11a]
GO:0006414 - translational elongation Inferred by computational analysis [UniProtGOA11a, Gaudet10, GOA06, GOA01a]
Molecular Function: GO:0005085 - guanyl-nucleotide exchange factor activity Inferred from experiment [Gromadski02]
GO:0005515 - protein binding Inferred from experiment [Lasserre06, Arifuzzaman06, Butland05, Kawashima96]
GO:0008270 - zinc ion binding Inferred from experiment [Katayama02]
GO:0003746 - translation elongation factor activity Inferred by computational analysis [UniProtGOA11a, Gaudet10, GOA06, GOA01a]
Cellular Component: GO:0005737 - cytoplasm Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06, Lasserre06]
GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, Zhang07a, LopezCampistrou05]
GO:0016020 - membrane Inferred from experiment [Lasserre06]
GO:0005622 - intracellular Inferred by computational analysis [GOA01a]

MultiFun Terms: information transfer protein related translation

Essentiality data for tsf knockouts: ?

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

Last-Curated ? 04-Apr-2013 by Keseler I , SRI International

Sequence Features

Protein sequence of protein chain elongation factor EF-Ts with features indicated

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[Pasquali94, Wilkins98, Link97, UniProt12a]
UniProt: Removed.
Chain 2 -> 283
UniProt: Elongation factor Ts;
Mutagenesis-Variant 24
[Zhang98b, UniProt11a]
UniProt: No change in binding to EF-Tu and in promoting GDP exchange.
Protein-Segment 80 -> 83
UniProt: Involved in Mg(2+) ion dislocation from EF-Tu; Sequence Annotation Type: region of interest;
Mutagenesis-Variant 81
[Zhang98b, UniProt11a]
UniProt: 2 to 3-fold less active in promoting GDP exchange and slightly lower binding constant for interaction with EF- Tu.
Mutagenesis-Variant 82
[Zhang98b, UniProt11a]
UniProt: 2 to 3-fold less active in promoting GDP exchange and 6-fold less active in binding to EF-Tu.
Acetylation-Modification 95
Mutagenesis-Variant 148
[Zhang98b, UniProt11a]
UniProt: At least 100-fold decrease in affinity between EF-Ts and EF-Tu and only small amount of GDP exchange activity.
Acetylation-Modification 247

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


10/20/97 Gene b0170 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11033; confirmed by SwissProt match.


Alexander95: Alexander C, Bilgin N, Lindschau C, Mesters JR, Kraal B, Hilgenfeld R, Erdmann VA, Lippmann C (1995). "Phosphorylation of elongation factor Tu prevents ternary complex formation." J Biol Chem 270(24);14541-7. PMID: 7782317

An81: An G, Bendiak DS, Mamelak LA, Friesen JD (1981). "Organization and nucleotide sequence of a new ribosomal operon in Escherichia coli containing the genes for ribosomal protein S2 and elongation factor Ts." Nucleic Acids Res 1981;9(16);4163-72. PMID: 6272196

Andersen03: Andersen GR, Nissen P, Nyborg J (2003). "Elongation factors in protein biosynthesis." Trends Biochem Sci 28(8);434-41. PMID: 12932732

Arifuzzaman06: Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699

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

Blumenthal72: Blumenthal T, Landers TA, Weber K (1972). "Bacteriophage Q replicase contains the protein biosynthesis elongation factors EF Tu and EF Ts." Proc Natl Acad Sci U S A 69(5);1313-7. PMID: 4624757

Blumenthal76: Blumenthal T, Landers TA (1976). "Renaturation of a multisubunit multiactivity enzyme complex: recovery of phage Qbeta RNA replicase, EF-Tu, and EF-Ts activities after denaturation in urea." Biochemistry 15(2);422-5. PMID: 764866

Bogestrand95: Bogestrand S, Wiborg O, Thirup S, Nyborg J (1995). "Analysis and crystallization of a 25 kDa C-terminal fragment of cloned elongation factor Ts from Escherichia coli." FEBS Lett 368(1);49-54. PMID: 7615087

Burnett13: Burnett BJ, Altman RB, Ferrao R, Alejo JL, Kaur N, Kanji J, Blanchard SC (2013). "Elongation Factor-Ts Directly Facilitates the Formation and Disassembly of the Escherichia Coli Elongation Factor-Tu-GTP-Aminoacyl-tRNA Ternary Complex." J Biol Chem. PMID: 23539628

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

Chau81: Chau V, Romero G, Biltonen RL (1981). "Kinetic studies on the interactions of Escherichia coli K12 elongation factor Tu with GDP and elongation factor Ts." J Biol Chem 256(11);5591-6. PMID: 7016856

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

Gaudet10: Gaudet P, Livstone M, Thomas P (2010). "Annotation inferences using phylogenetic trees." PMID: 19578431

GOA01a: 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."

Gromadski02: Gromadski KB, Wieden HJ, Rodnina MV (2002). "Kinetic mechanism of elongation factor Ts-catalyzed nucleotide exchange in elongation factor Tu." Biochemistry 41(1);162-9. PMID: 11772013

Han07: Han KY, Song JA, Ahn KY, Park JS, Seo HS, Lee J (2007). "Enhanced solubility of heterologous proteins by fusion expression using stress-induced Escherichia coli protein, Tsf." FEMS Microbiol Lett 274(1);132-8. PMID: 17608803

Hwang89a: Hwang YW, Sanchez A, Miller DL (1989). "Mutagenesis of bacterial elongation factor Tu at lysine 136. A conserved amino acid in GTP regulatory proteins." J Biol Chem 264(14);8304-9. PMID: 2498311

Hwang97: Hwang YW, Sanchez A, Hwang MC, Miller DL (1997). "The role of cysteinyl residues in the activity of bacterial elongation factor Ts, a guanosine nucleotide dissociation protein." Arch Biochem Biophys 348(1);157-62. PMID: 9390186

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

Karring03: Karring H, Bjornsson A, Thirup S, Clark BF, Knudsen CR (2003). "Functional effects of deleting the coiled-coil motif in Escherichia coli elongation factor Ts." Eur J Biochem 270(21);4294-305. PMID: 14622294

Karring04: Karring H, Mathu SG, van Duin J, Clark BF, Kraal B, Knudsen CR (2004). "Qbeta-phage resistance by deletion of the coiled-coil motif in elongation factor Ts." J Biol Chem 279(3);1878-84. PMID: 14583631

Katayama02: Katayama A, Tsujii A, Wada A, Nishino T, Ishihama A (2002). "Systematic search for zinc-binding proteins in Escherichia coli." Eur J Biochem 269(9);2403-13. PMID: 11985624

Kawashima96: Kawashima T, Berthet-Colominas C, Wulff M, Cusack S, Leberman R (1996). "The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution." Nature 379(6565);511-8. PMID: 8596629

Kidmose10: Kidmose RT, Vasiliev NN, Chetverin AB, Andersen GR, Knudsen CR (2010). "Structure of the Qbeta replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins." Proc Natl Acad Sci U S A 107(24);10884-9. PMID: 20534494

Krab01: Krab IM, te Biesebeke R, Bernardi A, Parmeggiani A (2001). "Elongation factor Ts can act as a steric chaperone by increasing the solubility of nucleotide binding-impaired elongation factor-Tu." Biochemistry 40(29);8531-5. PMID: 11456491

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

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

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

LucasLenard66: Lucas-Lenard J, Lipmann F (1966). "Separation of three microbial amino acid polymerization factors." Proc Natl Acad Sci U S A 55(6);1562-6. PMID: 4289971

LucasLenard71: Lucas-Lenard J (1971). "Protein biosynthesis." Annu Rev Biochem 40;409-48. PMID: 4941237

Manchester04: Manchester KL (2004). "Determination of the kinetics of guanine nucleotide exchange on EF-Tu and EF-Ts: continuing uncertainties." Biochem Biophys Res Commun 314(1);1-5. PMID: 14715237

Miller69: Miller DL, Weissbach H (1969). "An interaction between the transfer factors required for protein synthesis." Arch Biochem Biophys 132(1);146-50. PMID: 4893410

Miyajima78: Miyajima A, Kaziro Y (1978). "Coordination of levels of elongation factors Tu, Ts, and G, and ribosomal protein SI in Escherichia coli." J Biochem 83(2);453-62. PMID: 344309

Pan11: Pan JY, Wu H, Liu X, Li PP, Li H, Wang SY, Peng XX (2011). "Complexome of Escherichia coli cytosolic proteins under normal native conditions." Mol Biosyst 7(9);2651-63. PMID: 21717022

Pasquali94: Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F. (1994). Data submission to UniProtKB on 1994-09.

Takeshita10: Takeshita D, Tomita K (2010). "Assembly of Q{beta} viral RNA polymerase with host translational elongation factors EF-Tu and -Ts." Proc Natl Acad Sci U S A 107(36);15733-8. PMID: 20798060

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.

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProt12a: UniProt Consortium (2012). "UniProt version 2012-02 released on 2012-02-29 00:00:00." Database.

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

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

Wieden02: Wieden HJ, Gromadski K, Rodnin D, Rodnina MV (2002). "Mechanism of elongation factor (EF)-Ts-catalyzed nucleotide exchange in EF-Tu. Contribution of contacts at the guanine base." J Biol Chem 277(8);6032-6. PMID: 11744709

Wieden10: Wieden HJ, Mercier E, Gray J, Steed B, Yawney D (2010). "A combined molecular dynamics and rapid kinetics approach to identify conserved three-dimensional communication networks in elongation factor Tu." Biophys J 99(11);3735-43. PMID: 21112298

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

Wittinghofer83: Wittinghofer A, Guariguata R, Leberman R (1983). "Bacterial elongation factor Ts: isolation and reactivity with elongation factor Tu." J Bacteriol 153(3);1266-71. PMID: 6681813

Wurmbach79: Wurmbach P, Nierhaus KH (1979). "Isolation of the protein synthesis elongation factors EF-Tu, EF-Ts, and EF-G from Escherichia coli." Methods Enzymol 60;593-606. PMID: 379535

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

Zhang96f: Zhang Y, Li X, Spremulli LL (1996). "Role of the conserved aspartate and phenylalanine residues in prokaryotic and mitochondrial elongation factor Ts in guanine nucleotide exchange." FEBS Lett 391(3);330-2. PMID: 8765000

Zhang97c: Zhang Y, Sun V, Spremulli LL (1997). "Role of domains in Escherichia coli and mammalian mitochondrial elongation factor Ts in the interaction with elongation factor Tu." J Biol Chem 272(35);21956-63. PMID: 9268331

Zhang98b: Zhang Y, Yu NJ, Spremulli LL (1998). "Mutational analysis of the roles of residues in Escherichia coli elongation factor Ts in the interaction with elongation factor Tu." J Biol Chem 273(8);4556-62. PMID: 9468511

Other References Related to Gene Regulation

Aseev08: Aseev LV, Levandovskaya AA, Tchufistova LS, Scaptsova NV, Boni IV (2008). "A new regulatory circuit in ribosomal protein operons: S2-mediated control of the rpsB-tsf expression in vivo." RNA 14(9):1882-94. PMID: 18648071

Aseev14: Aseev LV, Koledinskaya LS, Boni IV (2014). "Dissecting the extended "-10" Escherichia coli rpsB promoter activity and regulation in vivo." Biochemistry (Mosc) 79(8);776-84. PMID: 25365487

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

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Fri Sep 4, 2015, biocyc11.