Gene Symbol: EFT2
Description: elongation factor 2
Alias: elongation factor 2
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. Fichtner L, Jablonowski D, Schierhorn A, Kitamoto H, Stark M, Schaffrath R. Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification. Mol Microbiol. 2003;49:1297-307 pubmed
    ..Similarly, KAP120 deletion rescues cells from zymocin, suggesting that Elongator's TOT function requires NLS- and karyopherin-dependent nuclear import. ..
  2. Mayor T, Lipford J, Graumann J, Smith G, Deshaies R. Analysis of polyubiquitin conjugates reveals that the Rpn10 substrate receptor contributes to the turnover of multiple proteasome targets. Mol Cell Proteomics. 2005;4:741-51 pubmed
  3. Ortiz P, Ulloque R, Kihara G, Zheng H, Kinzy T. Translation elongation factor 2 anticodon mimicry domain mutants affect fidelity and diphtheria toxin resistance. J Biol Chem. 2006;281:32639-48 pubmed
    Eukaryotic elongation factor 2 (eEF2) mediates translocation in protein synthesis. The molecular mimicry model proposes that the tip of domain IV mimics the anticodon loop of tRNA...
  4. Mayor T, Graumann J, Bryan J, MacCoss M, Deshaies R. Quantitative profiling of ubiquitylated proteins reveals proteasome substrates and the substrate repertoire influenced by the Rpn10 receptor pathway. Mol Cell Proteomics. 2007;6:1885-95 pubmed
    ..This approach illustrates the feasibility of systems-level quantitative analysis to map enzyme-substrate networks in the UPS. ..
  5. Zhang Y, Liu S, Lajoie G, Merrill A. The role of the diphthamide-containing loop within eukaryotic elongation factor 2 in ADP-ribosylation by Pseudomonas aeruginosa exotoxin A. Biochem J. 2008;413:163-74 pubmed publisher
    eEF2 (eukaryotic elongation factor 2) contains a post-translationally modified histidine residue, known as diphthamide, which is the specific ADP-ribosylation target of diphtheria toxin, cholix toxin and Pseudomonas aeruginosa exotoxin A...
  6. Uthman S, Bär C, Scheidt V, Liu S, Ten Have S, Giorgini F, et al. The amidation step of diphthamide biosynthesis in yeast requires DPH6, a gene identified through mining the DPH1-DPH5 interaction network. PLoS Genet. 2013;9:e1003334 pubmed publisher
    Diphthamide is a highly modified histidine residue in eukaryal translation elongation factor 2 (eEF2) that is the target for irreversible ADP ribosylation by diphtheria toxin (DT)...
  7. Hitchcock A, Auld K, Gygi S, Silver P. A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery. Proc Natl Acad Sci U S A. 2003;100:12735-40 pubmed
    ..Interestingly, we also identified novel membrane-bound transcription factors that may be subject to ubiquitin/proteasome-mediated cleavage and activation at the ER membrane. ..
  8. 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. ..
  9. McCarthy J. Posttranscriptional control of gene expression in yeast. Microbiol Mol Biol Rev. 1998;62:1492-553 pubmed

More Information


  1. Dzialo M, Travaglini K, Shen S, Roy K, Chanfreau G, Loo J, et al. Translational roles of elongation factor 2 protein lysine methylation. J Biol Chem. 2014;289:30511-24 pubmed publisher
    ..cerevisiae, the product of the EFM3/YJR129C gene is responsible for the trimethylation of lysine 509 on elongation factor 2. Deletion of EFM3 or of the previously described EFM2 increases sensitivity to antibiotics that target ..
  2. Davydova E, Ho A, Malecki J, Moen A, Enserink J, Jakobsson M, et al. Identification and characterization of a novel evolutionarily conserved lysine-specific methyltransferase targeting eukaryotic translation elongation factor 2 (eEF2). J Biol Chem. 2014;289:30499-510 pubmed publisher
    ..family of protein MTases, and we here show that FAM86A catalyzes the trimethylation of eukaryotic elongation factor 2 (eEF2) on Lys-525...
  3. Starita L, Lo R, Eng J, von Haller P, Fields S. Sites of ubiquitin attachment in Saccharomyces cerevisiae. Proteomics. 2012;12:236-40 pubmed publisher
    ..However, such peptides with GG shifts have been difficult to discover. We identify 870 unique sites of ubiquitin attachment on 438 different proteins of the yeast Saccharomyces cerevisiae. ..
  4. Ziv I, Matiuhin Y, Kirkpatrick D, Erpapazoglou Z, Leon S, Pantazopoulou M, et al. A perturbed ubiquitin landscape distinguishes between ubiquitin in trafficking and in proteolysis. Mol Cell Proteomics. 2011;10:M111.009753 pubmed publisher
    ..We conclude that despite the shared use of the ubiquitin molecule, the two branches of the ubiquitin machinery--the ubiquitin-proteasome system and the ubiquitin trafficking system--were unevenly perturbed by expression of K0 ubiquitin. ..
  5. Gregio A, Cano V, Avaca J, Valentini S, Zanelli C. eIF5A has a function in the elongation step of translation in yeast. Biochem Biophys Res Commun. 2009;380:785-90 pubmed publisher
    ..Taken together, these results not only reinforce a role for eIF5A in translation but also strongly support a function for eIF5A in the elongation step of protein synthesis. ..
  6. Perentesis J, Phan L, Gleason W, LaPorte D, Livingston D, Bodley J. Saccharomyces cerevisiae elongation factor 2. Genetic cloning, characterization of expression, and G-domain modeling. J Biol Chem. 1992;267:1190-7 pubmed
    The elongation factor 2 (EF-2) genes of the yeast Saccharomyces cerevisiae have been cloned and characterized with the ultimate goal of gaining a better understanding of the mechanism and control of protein synthesis...
  7. Luz J, Georg R, Gomes C, Machado Santelli G, Oliveira C. Sdo1p, the yeast orthologue of Shwachman-Bodian-Diamond syndrome protein, binds RNA and interacts with nuclear rRNA-processing factors. Yeast. 2009;26:287-98 pubmed publisher
    ..Sdo1p binds RNA directly, suggesting that it may associate with the ribosomal subunits also through RNA interaction. ..
  8. Dias C, Garcia W, Zanelli C, Valentini S. eIF5A dimerizes not only in vitro but also in vivo and its molecular envelope is similar to the EF-P monomer. Amino Acids. 2013;44:631-44 pubmed publisher
    ..Moreover, the molecular envelope determined from the SAXS data shows that the eIF5A dimer is L-shaped and superimposable on the tRNA(Phe) tertiary structure, analogously to the EF-P monomer. ..
  9. Gómez Lorenzo M, Spahn C, Agrawal R, Grassucci R, Penczek P, Chakraburtty K, et al. Three-dimensional cryo-electron microscopy localization of EF2 in the Saccharomyces cerevisiae 80S ribosome at 17.5 A resolution. EMBO J. 2000;19:2710-8 pubmed
    ..The shape and position of domain IV of EF2 suggest that it might interact directly with P-site-bound tRNA. ..
  10. Bailleul P, Newnam G, Steenbergen J, Chernoff Y. Genetic study of interactions between the cytoskeletal assembly protein sla1 and prion-forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae. Genetics. 1999;153:81-94 pubmed
    ..We hypothesize that Sup35N is involved in regulatory interactions with intracellular structural networks, and [PSI] prion may be formed as a by-product of this process. ..
  11. Kamber R, Shoemaker C, Denic V. Receptor-Bound Targets of Selective Autophagy Use a Scaffold Protein to Activate the Atg1 Kinase. Mol Cell. 2015;59:372-81 pubmed publisher
    ..This regulatory logic is a key similarity between selective autophagy and bulk autophagy, which is initiated by a distinct Atg1 activation mechanism during starvation. ..