Gene Symbol: TEF1
Description: translation elongation factor EF-1 alpha
Alias: translation elongation factor EF-1 alpha
Species: Saccharomyces cerevisiae S288c
Products:     TEF1

Top Publications

  1. McCarthy J. Posttranscriptional control of gene expression in yeast. Microbiol Mol Biol Rev. 1998;62:1492-553 pubmed
  2. Gromadski K, Schümmer T, Strømgaard A, Knudsen C, Kinzy T, Rodnina M. Kinetics of the interactions between yeast elongation factors 1A and 1Balpha, guanine nucleotides, and aminoacyl-tRNA. J Biol Chem. 2007;282:35629-37 pubmed
    ..eEF1A.GTP binds Phe-tRNA(Phe) with a K(d) of 3 nm, whereas eEF1A.GDP shows no significant binding, indicating that eEF1A has similar tRNA binding properties as its prokaryotic homolog, EF-Tu. ..
  3. McGuire A, Mangroo D. Cex1p is a novel cytoplasmic component of the Saccharomyces cerevisiae nuclear tRNA export machinery. EMBO J. 2007;26:288-300 pubmed
    ..cerevisiae. They also suggest that Cex1p collects aminoacyl-tRNAs from the nuclear export receptors at the cytoplasmic side of the nuclear pore complex, and transfers them to eEF-1A using a channelling mechanism. ..
  4. Gross S, Kinzy T. Translation elongation factor 1A is essential for regulation of the actin cytoskeleton and cell morphology. Nat Struct Mol Biol. 2005;12:772-8 pubmed
    ..This demonstrates for the first time a direct consequence of eEF1A on cytoskeletal organization in vivo and the physiological significance of this interaction. ..
  5. Grosshans H, Hurt E, Simos G. An aminoacylation-dependent nuclear tRNA export pathway in yeast. Genes Dev. 2000;14:830-40 pubmed
    ..Our data show that tRNA aminoacylation and eEF-1A are required for efficient nuclear tRNA export in yeast and suggest coordination between the protein translation and the nuclear tRNA processing and transport machineries. ..
  6. Murthi A, Shaheen H, Huang H, Preston M, Lai T, Phizicky E, et al. Regulation of tRNA bidirectional nuclear-cytoplasmic trafficking in Saccharomyces cerevisiae. Mol Biol Cell. 2010;21:639-49 pubmed publisher
    ..Finally, we implicate Tef1, the yeast orthologue of translation elongation factor eEF1A, in the tRNA reexport process and show that its ..
  7. Li Z, Gonzalez P, Sasvari Z, Kinzy T, Nagy P. Methylation of translation elongation factor 1A by the METTL10-like See1 methyltransferase facilitates tombusvirus replication in yeast and plants. Virology. 2014;448:43-54 pubmed publisher
    ..Silencing of the plant ortholog of See1 methyltransferase also decreased tombusvirus RNA accumulation in Nicotiana benthamiana...
  8. Dzialo M, Travaglini K, Shen S, Loo J, Clarke S. A new type of protein lysine methyltransferase trimethylates Lys-79 of elongation factor 1A. Biochem Biophys Res Commun. 2014;455:382-9 pubmed publisher
    ..Further analysis of this motif and others like it demonstrates a potential consensus sequence for N-methyltransferases. ..
  9. Ansari H, Greco G, Luban J. Cyclophilin A peptidyl-prolyl isomerase activity promotes ZPR1 nuclear export. Mol Cell Biol. 2002;22:6993-7003 pubmed
    ..Our results demonstrate a functional interaction between Cpr1p, Zpr1p, and EF1alpha, a role for Cpr1p in Zpr1p nuclear export, and a biological function for Cpr1p PPIase activity. ..

More Information


  1. Nagashima K, Kasai M, Nagata S, Kaziro Y. Structure of the two genes coding for polypeptide chain elongation factor 1 alpha (EF-1 alpha) from Saccharomyces cerevisiae. Gene. 1986;45:265-73 pubmed
    ..The sequence which commonly exists in the 5'-flanking regions of ribosomal protein genes of S. cerevisiae was also present in the two EF1 alpha genes. ..
  2. Hamey J, Winter D, Yagoub D, Overall C, Hart Smith G, Wilkins M. Novel N-terminal and Lysine Methyltransferases That Target Translation Elongation Factor 1A in Yeast and Human. Mol Cell Proteomics. 2016;15:164-76 pubmed publisher
    ..This implies more extensive regulation of eEF1A by this posttranslational modification than previously appreciated. ..
  3. Olarewaju O, Ortiz P, Chowdhury W, Chatterjee I, Kinzy T. The translation elongation factor eEF1B plays a role in the oxidative stress response pathway. RNA Biol. 2004;1:89-94 pubmed
    ..As nucleotide exchange is a critical regulator of most G-proteins, these results indicate a new mechanism in the growing list of examples of post-transcriptional responses to cellular stress. ..
  4. Doyle A, Crosby S, Burton D, Lilley F, Murphy M. Actin bundling and polymerisation properties of eukaryotic elongation factor 1 alpha (eEF1A), histone H2A-H2B and lysozyme in vitro. J Struct Biol. 2011;176:370-8 pubmed publisher
  5. Kovalchuke O, Kambampati R, Pladies E, Chakraburtty K. Competition and cooperation amongst yeast elongation factors. Eur J Biochem. 1998;258:986-93 pubmed
    ..These results strongly suggest that the stimulatory effect of EF-3 on the ternary complex binding to yeast ribosomes involves a direct interaction between EF-1 alpha and EF-3. ..
  6. Laxman S, Tu B. Multiple TORC1-associated proteins regulate nitrogen starvation-dependent cellular differentiation in Saccharomyces cerevisiae. PLoS ONE. 2011;6:e26081 pubmed publisher
    ..Our studies also suggest the CEN.PK strain background of S. cerevisiae may be particularly useful for investigations of nitrogen starvation-induced diploid pseudohyphal growth. ..
  7. Carr Schmid A, Durko N, Cavallius J, Merrick W, Kinzy T. Mutations in a GTP-binding motif of eukaryotic elongation factor 1A reduce both translational fidelity and the requirement for nucleotide exchange. J Biol Chem. 1999;274:30297-302 pubmed
    ..Additionally, eEF1A mutations that suppress the requirement for guanine nucleotide exchange may not effectively perform all the functions of eEF1A in vivo. ..
  8. Brandina I, Graham J, Lemaitre Guillier C, Entelis N, Krasheninnikov I, Sweetlove L, et al. Enolase takes part in a macromolecular complex associated to mitochondria in yeast. Biochim Biophys Acta. 2006;1757:1217-28 pubmed
    ..This suggests an unsuspected novel function for this complex in tRNA mitochondrial import. ..
  9. Gemayel R, Chavali S, Pougach K, Legendre M, Zhu B, Boeynaems S, et al. Variable Glutamine-Rich Repeats Modulate Transcription Factor Activity. Mol Cell. 2015;59:615-27 pubmed publisher
    ..Thus, Q-rich repeats are dynamic functional domains that modulate a regulator's innate function, with the inherent risk of pathogenic repeat expansions. ..
  10. Mishra A, Gangwani L, Davis R, Lambright D. Structural insights into the interaction of the evolutionarily conserved ZPR1 domain tandem with eukaryotic EF1A, receptors, and SMN complexes. Proc Natl Acad Sci U S A. 2007;104:13930-5 pubmed
    ..Structural differences between the ZPR1 domains contribute to the observed functional divergence and provide evidence for distinct modalities of interaction with eEF1A and survival motor neuron complexes. ..
  11. Hsieh C, Huang S, Wu Y, Liu L, Han C, Liu Y, et al. Expression of proteins with dimethylarginines in Escherichia coli for protein-protein interaction studies. Protein Sci. 2007;16:919-28 pubmed
    ..Sbp1p and Sbp1p/hmt1 were covalently attached to solid supports for the isolation of interacting proteins. The results indicate that arginine methylation on Sbp1p exerts both positive and negative effects on protein-protein interaction. ..
  12. Jakobsson M, Davydova E, Małecki J, Moen A, Falnes P. Saccharomyces cerevisiae Eukaryotic Elongation Factor 1A (eEF1A) Is Methylated at Lys-390 by a METTL21-Like Methyltransferase. PLoS ONE. 2015;10:e0131426 pubmed publisher
    ..Our results demonstrate that Ynl024c is the enzyme responsible for methylation of eEF1A at Lys390, and in accordance with prior naming of similar enzymes, we suggest that Ynl024c is renamed to Efm6 (Elongation factor MTase 6). ..
  13. Honey S, Schneider B, Schieltz D, Yates J, Futcher B. A novel multiple affinity purification tag and its use in identification of proteins associated with a cyclin-CDK complex. Nucleic Acids Res. 2001;29:E24 pubmed
    ..Associated proteins were identified using mass spectrometry. These included the known associated proteins Cdc28, Sic1 and Cks1. Several other proteins were found including the 70 kDa chaperone, Ssa1. ..
  14. Daugeron M, Prouteau M, Lacroute F, Seraphin B. The highly conserved eukaryotic DRG factors are required for efficient translation in a manner redundant with the putative RNA helicase Slh1. Nucleic Acids Res. 2011;39:2221-33 pubmed publisher
  15. Visweswaraiah J, Lageix S, Castilho B, Izotova L, Kinzy T, Hinnebusch A, et al. Evidence that eukaryotic translation elongation factor 1A (eEF1A) binds the Gcn2 protein C terminus and inhibits Gcn2 activity. J Biol Chem. 2011;286:36568-79 pubmed publisher
    ..These findings implicate eEF1A in the intricate regulation of Gcn2 and amino acid homeostasis. ..
  16. Naticchia M, Brown H, Garcia F, Lamade A, Justice S, Herrin R, et al. Bifunctional electrophiles cross-link thioredoxins with redox relay partners in cells. Chem Res Toxicol. 2013;26:490-7 pubmed publisher
    ..Taken together, our results indicate that bifunctional electrophiles potentially disrupt redox homeostasis in yeast and human cells by forming cross-linked complexes between thioredoxins and their redox partners. ..
  17. Cottrelle P, Cool M, Thuriaux P, Price V, Thiele D, Buhler J, et al. Either one of the two yeast EF-1 alpha genes is required for cell viability. Curr Genet. 1985;9:693-7 pubmed
    Two genes, TEF1 and TEF2, encode the protein elongation factor EF-1 alpha in the yeast Saccharomyces cerevisiae...
  18. Ozturk S, Kinzy T. Guanine nucleotide exchange factor independence of the G-protein eEF1A through novel mutant forms and biochemical properties. J Biol Chem. 2008;283:23244-53 pubmed publisher
    ..The biochemical properties of these eEF1A mutants provide insight into the mechanism behind GEF-independent G-protein function. ..
  19. Huang H, Hopper A. In vivo biochemical analyses reveal distinct roles of β-importins and eEF1A in tRNA subcellular traffic. Genes Dev. 2015;29:772-83 pubmed publisher
    ..b>Tef1/2 (the yeast form of translation elongation factor 1α [eEF1A]) aids the specificity of Msn5 for aminoacylated ..
  20. Sobti M, Cubeddu L, Haynes P, Mabbutt B. Engineered rings of mixed yeast Lsm proteins show differential interactions with translation factors and U-rich RNA. Biochemistry. 2010;49:2335-45 pubmed publisher
    ..Our findings suggest Lsm1 and/or Lsm4 can interact with translationally active mRNA. ..
  21. Lipson R, Webb K, Clarke S. Two novel methyltransferases acting upon eukaryotic elongation factor 1A in Saccharomyces cerevisiae. Arch Biochem Biophys. 2010;500:137-43 pubmed publisher
    ..We suggest that YHL039W (now designated EFM1 for elongation factor methyltransferase 1) and YIL064W/SEE1 encode distinct eEF1A methyltransferases that respectively monomethylate and dimethylate this protein at lysine residues. ..
  22. Möckli N, Deplazes A, Hassa P, Zhang Z, Peter M, Hottiger M, et al. Yeast split-ubiquitin-based cytosolic screening system to detect interactions between transcriptionally active proteins. Biotechniques. 2007;42:725-30 pubmed
    ..The cytoY2H system extends existing methods for the detection of protein interactions by providing a convenient solution for screening a wide range of transcriptionally active proteins. ..
  23. Panni S, Montecchi Palazzi L, Kiemer L, Cabibbo A, Paoluzi S, Santonico E, et al. Combining peptide recognition specificity and context information for the prediction of the 14-3-3-mediated interactome in S. cerevisiae and H. sapiens. Proteomics. 2011;11:128-43 pubmed publisher
    ..Our approach provides an orthogonal reliability assessment and maps with high confidence the 14-3-3 peptide target on the partner proteins. ..
  24. Krokowski D, Tchorzewski M, Boguszewska A, McKay A, Maslen S, Robinson C, et al. Elevated copy number of L-A virus in yeast mutant strains defective in ribosomal stalk. Biochem Biophys Res Commun. 2007;355:575-80 pubmed
  25. Dewe J, Whipple J, Chernyakov I, Jaramillo L, Phizicky E. The yeast rapid tRNA decay pathway competes with elongation factor 1A for substrate tRNAs and acts on tRNAs lacking one or more of several modifications. RNA. 2012;18:1886-96 pubmed publisher
    ..These results demonstrate that RTD interacts with the translation machinery and acts widely on hypomodified tRNAs. ..
  26. Chakraburtty K, Triana Alonso F. Yeast elongation factor 3: structure and function. Biol Chem. 1998;379:831-40 pubmed
    ..EF-3 function is dependent on ATP hydrolysis. The existence of functional homologs of EF-3 in higher eukaryotes is still an open question. Further investigations are needed to settle this issue. ..
  27. Waller T, Lee S, Sattlegger E. Evidence that Yih1 resides in a complex with ribosomes. FEBS J. 2012;279:1761-76 pubmed publisher
    ..Close physical proximity of Yih1 to the Gcn1-Gcn2-ribosome complex would allow cells to quickly inhibit Gcn2 whenever or wherever necessary. ..
  28. Belyi Y, Tartakovskaya D, Tais A, Fitzke E, Tzivelekidis T, Jank T, et al. Elongation factor 1A is the target of growth inhibition in yeast caused by Legionella pneumophila glucosyltransferase Lgt1. J Biol Chem. 2012;287:26029-37 pubmed publisher
    ..cerevisiae. Our data indicate that Lgt1-induced lethal effect in yeast depends solely on eEF1A. The region of eEF1A encompassing serine 53 plays a critical role in functioning of the elongation factor...
  29. Pittman Y, Kandl K, Lewis M, Valente L, Kinzy T. Coordination of eukaryotic translation elongation factor 1A (eEF1A) function in actin organization and translation elongation by the guanine nucleotide exchange factor eEF1Balpha. J Biol Chem. 2009;284:4739-47 pubmed publisher
    ..The consequences of the overlapping functions in this eEF1A domain and its unique differences from the bacterial homologs provide a novel function for eEF1Balpha to balance the dual roles in actin bundling and protein synthesis. ..
  30. Drummond S, Hildyard J, Firczuk H, Reamtong O, Li N, Kannambath S, et al. Diauxic shift-dependent relocalization of decapping activators Dhh1 and Pat1 to polysomal complexes. Nucleic Acids Res. 2011;39:7764-74 pubmed publisher
    ..This reveals a new dimension to the relationship between translation activity and interactions between mRNA, the translation machinery and decapping activator proteins. ..
  31. Lee R, Brunette S, Puente L, Megeney L. Metacaspase Yca1 is required for clearance of insoluble protein aggregates. Proc Natl Acad Sci U S A. 2010;107:13348-53 pubmed publisher
    ..Together, our results show that Yca1 contributes to the fitness and adaptability of growing yeast through an aggregate remodeling activity. ..
  32. Jao D, Chen K. Tandem affinity purification revealed the hypusine-dependent binding of eukaryotic initiation factor 5A to the translating 80S ribosomal complex. J Cell Biochem. 2006;97:583-98 pubmed
  33. Ranish J, Yi E, Leslie D, Purvine S, Goodlett D, Eng J, et al. The study of macromolecular complexes by quantitative proteomics. Nat Genet. 2003;33:349-55 pubmed
  34. Pedersen L, Andersen G, Knudsen C, Kinzy T, Nyborg J. Crystallization of the yeast elongation factor complex eEF1A-eEF1B alpha. Acta Crystallogr D Biol Crystallogr. 2001;57:159-61 pubmed
  35. Umikawa M, Tanaka K, Kamei T, Shimizu K, Imamura H, Sasaki T, et al. Interaction of Rho1p target Bni1p with F-actin-binding elongation factor 1alpha: implication in Rho1p-regulated reorganization of the actin cytoskeleton in Saccharomyces cerevisiae. Oncogene. 1998;16:2011-6 pubmed
    ..These results suggest that the Rho1p-Bni1p system regulates reorganization of the actin cytoskeleton through the interaction with both EF1alpha and profilin. ..
  36. Reineke L, Cao Y, Baus D, Hossain N, Merrick W. Insights into the role of yeast eIF2A in IRES-mediated translation. PLoS ONE. 2011;6:e24492 pubmed publisher
    ..These data suggest that eIF2A acts as a switch to regulate IRES-mediated translation, and eEF1A may be an important mediator of translational activation during ethanol stress. ..
  37. Perez W, Kinzy T. Translation elongation factor 1A mutants with altered actin bundling activity show reduced aminoacyl-tRNA binding and alter initiation via eIF2? phosphorylation. J Biol Chem. 2014;289:20928-38 pubmed
    ..The eEF1A actin-bundling proteins exhibit changes in their elongation activity at the level of aminoacyl-tRNA binding in vitro. These findings implicate eEF1A in a feedback mechanism for regulating translation at initiation. ..
  38. Bodman J, Yang Y, Logan M, Eitzen G. Yeast translation elongation factor-1A binds vacuole-localized Rho1p to facilitate membrane integrity through F-actin remodeling. J Biol Chem. 2015;290:4705-16 pubmed publisher
    ..Here, we identified eEF1A as a vacuolar Rho1p-interacting protein. eEF1A (encoded by the TEF1 and TEF2 genes in yeast) is an aminoacyl-tRNA transferase needed during protein translation...
  39. Chuang S, Chen L, Lambertson D, Anand M, Kinzy T, Madura K. Proteasome-mediated degradation of cotranslationally damaged proteins involves translation elongation factor 1A. Mol Cell Biol. 2005;25:403-13 pubmed
    ..Our findings provide a mechanistic foundation for defining how cellular proteins are degraded cotranslationally. ..
  40. Miao Y, Han X, Zheng L, Xie Y, Mu Y, Yates J, et al. Fimbrin phosphorylation by metaphase Cdk1 regulates actin cable dynamics in budding yeast. Nat Commun. 2016;7:11265 pubmed publisher
    ..Overall, this work identifies fimbrin as a key target for cell cycle regulation of actin cable assembly in budding yeast, and suggests an underlying mechanism. ..