The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

TSFM  -  Ts translation elongation factor,...

Homo sapiens

Synonyms: EF-TS, EF-Ts, EF-TsMt, EF-Tsmt, EFTS, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of TSFM

  • Both the mature and precursor forms of bovine liver EF-Tsmt have been expressed in E. coli as histidine-tagged proteins [1].
  • The effects of either trastuzumab, CIK cells alone, or CD3xHer2/neu bispecific antibody redirected CIK cells was determined using a SCID/hu model of EFTs and serial, noninvasive bioluminescent imaging [2].
  • Thus, efts have a variety of behaviors that reduce the risk of dehydration associated with climate change [3].
  • Between October 1989 and November 1998, 822 patients with a clinical diagnosis of GERD (based on symptoms and endoscopic findings) were referred for EFTs [4].
  • METHODS: The study was performed on a series of 27 EFTs (osseous Ewing's sarcoma, 18 cases; extraosseous Ewing's sarcoma, 2; peripheral neuroepithelioma, 4; Askin Rosai tumors, 3) [5].

High impact information on TSFM

  • The most important effects are: (i) a strong reduction of the intrinsic GTPase activity, (ii) a remarkable enhancement of the association and dissociation rates of EF-TuGly20-GDP, mimicking the effect of elongation factor Ts (EF-Ts) and (iii) the inability of ribosomes to influence the intrinsic GTPase of EF-Tu uncoupled from poly(Phe) synthesis [6].
  • As with the latter, poly(Phe) synthesis by EF-TuGly20 is inhibited by the antibiotic kirromycin, but differs remarkably in that it is largely independent of the presence of EF-Ts [6].
  • EFTs functions as a guanine nucleotide exchange factor for EFTu, another translation elongation factor that brings aminoacylated transfer RNAs to the ribosomal A site as a ternary complex with guanosine triphosphate [7].
  • The steady-state levels of EFTs and EFTu in patient fibroblasts were reduced by 75% and 60%, respectively, and the amounts of assembled complexes I, IV, and V were reduced by 35%-91% compared with the amounts in controls [7].
  • These phenotypes and the translation defect were rescued by retroviral expression of either EFTs or EFTu [7].

Biological context of TSFM


Anatomical context of TSFM

  • Northern analysis using a human multiple tissue blot indicates that EF-Tsmt is expressed in all tissues, with the highest levels of expression in skeletal muscle, liver, and kidney [1].
  • Whereas EF-Ts is lacking in S. cerevisiae, both translation factors are found in S. pombe and H. sapiens mitochondria, consistent with the known similarity between fission yeast and human cell mitochondrial physiology [12].
  • In this study we show that the inhibition of protein synthesis by MDL 62,879 in an Escherichia coli cell-free system was fully reversed by addition of stoichiometric amounts of EF-Tu but not by large excesses of EF-Ts, ribosomes, or aa-tRNA [13].
  • Right upper limbs of 20 efts were examined at low magnification to establish carpal composition and organization [14].
  • Delayed carpal ossification in Notophthalmus viridescens Efts: Relation to the progress of mesopodial completion in newt forelimb regenerates [14].

Associations of TSFM with chemical compounds

  • Two of these polypeptides, protein synthesis elongation factors EF-Tu and EF-Ts, can be covalently crosslinked with dimethyl suberimidate to form a complex which lacks the ability to catalyze the known host functions catalyzed by the individual elongation factors [15].
  • The trypsin-cleaved EF-Tu still can bind GDP and EF-Ts and can function in Qbeta replicase, but it no longer spontaneously renatures following denaturation in urea [9].
  • GDP is a competitive inhibitor of IDP exchange, a result predicted for the substituted enzyme mechanism but inconsistent with ternary complex mechanisms that involve an intermediate complex containing EF-Ts and both substrates [16].
  • The effects of pulvomycin and EF-Ts can coexist and are simply additive, supporting the conclusion that these two ligands interact with different sites of EF-Tu [17].
  • Steady-state and dynamic polarization measurements revealed limited local mobility for the tryptophan in the EF-Tu x GDP complex whereas formation of the EF-Tu x EF-Ts complex led to a dramatic increase in this local mobility [18].

Physical interactions of TSFM

  • Asp83 has a conformation similar to the conformation of the corresponding residue in the EF-Tu/EF-Ts complex [19].

Regulatory relationships of TSFM

  • In the wheat system, however, both EF-1b and EF-1b' had the EF-Ts-like activity to stimulate EF-1a-dependent binding of aminoacyl-tRNA to ribosomes [20].

Other interactions of TSFM

  • EF-Tu/GDP is recycled by the guanine nucleotide exchange factor EF-Ts [12].
  • Renaturation of rhodanese and GTP hydrolysis by EF-Tu are greatly enhanced by the guanine nucleotide exchange factor EF-Ts [10].
  • In agreement with studies on EF-Ts and human EF-1beta, a functional mechanism for nucleotide exchange is proposed wherein Phe46 on an exposed loop acts as a lever to eject GDP from the associated elongation factor G-protein, aEF-1alpha. aEF-1beta was also found to bind calcium in the groove between helix alpha2 and strand beta4 [21].
  • In the animal system, EF-1a and EF-1b correspond functionally to EF-Tu and EF-Ts, respectively [20].

Analytical, diagnostic and therapeutic context of TSFM

  • When exposed to combined desiccation and predation risks, efts were less active than when exposed to either risk separately and avoided adult tissue extracts, but not eft extracts [3].
  • Interactions of EF-Ts with EF-Tu at all steps of the elongation cycle were studied by limited trypsinolysis, gel-filtration, analytical centrifugation and fluorescence polarization techniques [22].
  • Esophageal function tests (EFTs: esophageal manometry and 24-hr pH monitoring) are generally reserved for patients who have the most severe disease, including those being considered for surgery [4].
  • We hypothesized that EFTs are more accurate than symptoms and endoscopy in the diagnosis of GERD [4].
  • EFTs are characterized by specific chromosomal translocations that result in chimeric transcripts that can be detected with reverse transcriptase-polymerase chain reaction (RT-PCR) analysis [23].


  1. Cloning and expression of mitochondrial translational elongation factor Ts from bovine and human liver. Xin, H., Woriax, V., Burkhart, W., Spremulli, L.L. J. Biol. Chem. (1995) [Pubmed]
  2. Low levels of Her2/neu expressed by Ewing's family tumor cell lines can redirect cytokine-induced killer cells. Verneris, M.R., Arshi, A., Edinger, M., Kornacker, M., Natkunam, Y., Karami, M., Cao, Y.A., Marina, N., Contag, C.H., Negrin, R.S. Clin. Cancer Res. (2005) [Pubmed]
  3. Dryness increases predation risk in efts: support for an amphibian decline hypothesis. Rohr, J.R., Madison, D.M. Oecologia (2003) [Pubmed]
  4. Role of esophageal function tests in diagnosis of gastroesophageal reflux disease. Patti, M.G., Diener, U., Tamburini, A., Molena, D., Way, L.W. Dig. Dis. Sci. (2001) [Pubmed]
  5. Retrospective analysis of ploidy in primary osseous and extraosseous Ewing family tumors in children. Perotti, D., Corletto, V., Giardini, R., Parafioriti, A., Fossati-Bellani, F., Luksch, R. Tumori. (1998) [Pubmed]
  6. Structure-function relationships in the GTP binding domain of EF-Tu: mutation of Val20, the residue homologous to position 12 in p21. Jacquet, E., Parmeggiani, A. EMBO J. (1988) [Pubmed]
  7. Distinct Clinical Phenotypes Associated with a Mutation in the Mitochondrial Translation Elongation Factor EFTs. Smeitink, J.A., Elpeleg, O., Antonicka, H., Diepstra, H., Saada, A., Smits, P., Sasarman, F., Vriend, G., Jacob-Hirsch, J., Shaag, A., Rechavi, G., Welling, B., Horst, J., Rodenburg, R.J., van den Heuvel, B., Shoubridge, E.A. Am. J. Hum. Genet. (2006) [Pubmed]
  8. Assignment of the mitochondrial translation elongation factor Ts gene (TSFM) to human chromosome 12 bands q13-->q14 by in situ hybridization and with somatic cell hybrids. Vernon, J.L., Burr, P.C., Wiley, J.E., Farwell, M.A. Cytogenet. Cell Genet. (2000) [Pubmed]
  9. Conformational alteration of protein synthesis elongation factor EF-Tu by EF-Ts and by kirromycin. Blumenthal, T., Douglass, J., Smith, D. Proc. Natl. Acad. Sci. U.S.A. (1977) [Pubmed]
  10. Renaturation of rhodanese by translational elongation factor (EF) Tu. Protein refolding by EF-Tu flexing. Kudlicki, W., Coffman, A., Kramer, G., Hardesty, B. J. Biol. Chem. (1997) [Pubmed]
  11. Kinetics and thermodynamics of the interaction of elongation factor Tu with elongation factor Ts, guanine nucleotides, and aminoacyl-tRNA. Romero, G., Chau, V., Biltonen, R.L. J. Biol. Chem. (1985) [Pubmed]
  12. Mitochondrial translation: elongation factor tu is essential in fission yeast and depends on an exchange factor conserved in humans but not in budding yeast. Chiron, S., Suleau, A., Bonnefoy, N. Genetics (2005) [Pubmed]
  13. Antibiotics MDL 62,879 and kirromycin bind to distinct and independent sites of elongation factor Tu (EF-Tu). Landini, P., Soffientini, A., Monti, F., Lociuro, S., Marzorati, E., Islam, K. Biochemistry (1996) [Pubmed]
  14. Delayed carpal ossification in Notophthalmus viridescens Efts: Relation to the progress of mesopodial completion in newt forelimb regenerates. Libbin, R.M., Mitchell, O.G., Guerra, L., Person, P. J. Exp. Zool. (1989) [Pubmed]
  15. Reconstitution of Qbeta RNA replicase from a covalently bonded elongation factor Tu-Ts complex. Brown, S., Blumenthal, T. Proc. Natl. Acad. Sci. U.S.A. (1976) [Pubmed]
  16. A study of the kinetic mechanism of elongation factor Ts. Hwang, Y.W., Miller, D.L. J. Biol. Chem. (1985) [Pubmed]
  17. Effects of the antibiotic pulvomycin on the elongation factor Tu-dependent reactions. Comparison with other antibiotics. Anborgh, P.H., Okamura, S., Parmeggiani, A. Biochemistry (2004) [Pubmed]
  18. Intrinsic fluorescence of elongation factor Tu in its complexes with GDP and elongation factor Ts. Jameson, D.M., Gratton, E., Eccleston, J.F. Biochemistry (1987) [Pubmed]
  19. The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange. al-Karadaghi, S., Aevarsson, A., Garber, M., Zheltonosova, J., Liljas, A. Structure (1996) [Pubmed]
  20. Occurrence of four subunits in high molecular weight forms of polypeptide chain elongation factor 1 from wheat embryo. Ejiri, S., Ebata, N., Kawamura, R., Katsumata, T. J. Biochem. (1983) [Pubmed]
  21. Rapid fold and structure determination of the archaeal translation elongation factor 1beta from Methanobacterium thermoautotrophicum. Kozlov, G., Ekiel, I., Beglova, N., Yee, A., Dharamsi, A., Engel, A., Siddiqui, N., Nong, A., Gehring, K. J. Biomol. NMR (2000) [Pubmed]
  22. Novel data on interactions of elongation factor Ts. Bubunenko, M.G., Kireeva, M.L., Gudkov, A.T. Biochimie (1992) [Pubmed]
  23. The predictive potential of molecular detection in the nonmetastatic Ewing family of tumors. Avigad, S., Cohen, I.J., Zilberstein, J., Liberzon, E., Goshen, Y., Ash, S., Meller, I., Kollender, Y., Issakov, J., Zaizov, R., Yaniv, I. Cancer (2004) [Pubmed]
WikiGenes - Universities