Gene Symbol: HYP2
Description: translation elongation factor eIF-5A
Alias: TIF51A, translation elongation factor eIF-5A
Species: Saccharomyces cerevisiae S288c
Products:     HYP2

Top Publications

  1. ElAntak L, Wagner S, Herrmannová A, Karásková M, Rutkai E, Lukavsky P, et al. The indispensable N-terminal half of eIF3j/HCR1 cooperates with its structurally conserved binding partner eIF3b/PRT1-RRM and with eIF1A in stringent AUG selection. J Mol Biol. 2010;396:1097-116 pubmed publisher
    ..Taken together, we propose that eIF3j/HCR1 closely cooperates with the eIF3b/PRT1 RRM and eIF1A on the ribosome to ensure proper formation of the scanning-arrested conformation required for stringent AUG recognition. ..
  2. Zanelli C, Valentini S. Pkc1 acts through Zds1 and Gic1 to suppress growth and cell polarity defects of a yeast eIF5A mutant. Genetics. 2005;171:1571-81 pubmed
    ..We have previously shown that high-copy PKC1 suppresses the phenotype of tif51A-1, a temperature-sensitive mutant of eIF5A in S. cerevisiae...
  3. Dias C, Cano V, Rangel S, Apponi L, Frigieri M, Muniz J, et al. Structural modeling and mutational analysis of yeast eukaryotic translation initiation factor 5A reveal new critical residues and reinforce its involvement in protein synthesis. FEBS J. 2008;275:1874-88 pubmed publisher
    ..Our data revealed important structural features of eIF5A that are required for its vital role in cell viability and underscored an essential function of eIF5A in the translation step of gene expression. ..
  4. Cuchalová L, Kouba T, Herrmannová A, Dányi I, Chiu W, Valásek L. The RNA recognition motif of eukaryotic translation initiation factor 3g (eIF3g) is required for resumption of scanning of posttermination ribosomes for reinitiation on GCN4 and together with eIF3i stimulates linear scanning. Mol Cell Biol. 2010;30:4671-86 pubmed publisher
    ..Together these results implicate g/Tif35 and i/Tif34 in stimulation of linear scanning and, specifically in the case of g/Tif35, also in proper regulation of the GCN4 reinitiation mechanism. ..
  5. Henderson A, Hershey J. Eukaryotic translation initiation factor (eIF) 5A stimulates protein synthesis in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 2011;108:6415-9 pubmed publisher
    ..This discrepancy is discussed...
  6. Kouba T, Rutkai E, Karásková M, Valášek L. The eIF3c/NIP1 PCI domain interacts with RNA and RACK1/ASC1 and promotes assembly of translation preinitiation complexes. Nucleic Acids Res. 2012;40:2683-99 pubmed publisher
  7. Saini P, Eyler D, Green R, Dever T. Hypusine-containing protein eIF5A promotes translation elongation. Nature. 2009;459:118-21 pubmed publisher
    ..The factor eIF5A (encoded by HYP2 and ANB1 in Saccharomyces cerevisiae), the sole protein in eukaryotes and archaea to contain the unusual amino acid ..
  8. 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. ..
  9. Valentini S, Casolari J, Oliveira C, Silver P, McBride A. Genetic interactions of yeast eukaryotic translation initiation factor 5A (eIF5A) reveal connections to poly(A)-binding protein and protein kinase C signaling. Genetics. 2002;160:393-405 pubmed
    ..To further our understanding of this essential protein, three temperature-sensitive alleles of the yeast TIF51A gene have been characterized...

More Information


  1. 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
    ..The TAP-tag was fused in-frame to chromosomal TIF51A gene and eIF5A-TAP fusion protein expressed at its natural level was used as the bait to fish out its interacting ..
  2. Thompson G, Cano V, Valentini S. Mapping eIF5A binding sites for Dys1 and Lia1: in vivo evidence for regulation of eIF5A hypusination. FEBS Lett. 2003;555:464-8 pubmed
    ..We suggest that this inhibition be abrogated in the cell when hypusinated and functional eIF5A is required. ..
  3. Chiu W, Wagner S, Herrmannová A, Burela L, Zhang F, Saini A, et al. The C-terminal region of eukaryotic translation initiation factor 3a (eIF3a) promotes mRNA recruitment, scanning, and, together with eIF3j and the eIF3b RNA recognition motif, selection of AUG start codons. Mol Cell Biol. 2010;30:4415-34 pubmed publisher
  4. Schmidt C, Becker T, Heuer A, Braunger K, Shanmuganathan V, Pech M, et al. Structure of the hypusinylated eukaryotic translation factor eIF-5A bound to the ribosome. Nucleic Acids Res. 2016;44:1944-51 pubmed publisher
    ..These findings would support a model whereby eIF-5A stimulates peptide bond formation on polyproline-stalled ribosomes by stabilizing and orienting the CCA-end of the P-tRNA, rather than by directly contributing to the catalysis. ..
  5. Wilson Zbinden C, Dos Santos A, Stoffel Studer I, van der Vaart A, Hofmann K, Reggiori F, et al. Autophagy competes for a common phosphatidylethanolamine pool with major cellular PE-consuming pathways in Saccharomyces cerevisiae. Genetics. 2015;199:475-85 pubmed publisher
  6. Pelechano V, Alepuz P. eIF5A facilitates translation termination globally and promotes the elongation of many non polyproline-specific tripeptide sequences. Nucleic Acids Res. 2017;45:7326-7338 pubmed publisher
    ..Our results support a broad mRNA-specific role of eIF5A in translation and identify the conserved motifs that affect translation elongation from yeast to humans. ..
  7. Windgassen M, Sturm D, Cajigas I, Gonzalez C, Seedorf M, Bastians H, et al. Yeast shuttling SR proteins Npl3p, Gbp2p, and Hrb1p are part of the translating mRNPs, and Npl3p can function as a translational repressor. Mol Cell Biol. 2004;24:10479-91 pubmed
    ..Together, these data shed light onto the transformation of an exporting to a translating mRNP. ..
  8. Morehouse H, Buratowski R, Silver P, Buratowski S. The importin/karyopherin Kap114 mediates the nuclear import of TATA-binding protein. Proc Natl Acad Sci U S A. 1999;96:12542-7 pubmed
    ..One suppressor was TIF51A, which encodes eukaryotic translation initiation factor 5A...
  9. Schuller A, Wu C, Dever T, Buskirk A, Green R. eIF5A Functions Globally in Translation Elongation and Termination. Mol Cell. 2017;66:194-205.e5 pubmed publisher
    ..We conclude that eIF5A functions broadly in elongation and termination, rationalizing its high cellular abundance and essential nature. ..
  10. Jennings M, Pavitt G. eIF5 has GDI activity necessary for translational control by eIF2 phosphorylation. Nature. 2010;465:378-81 pubmed publisher
    ..Together our studies define a new step in the translation initiation pathway, one that is critical for normal translational controls. ..
  11. Schnier J, Schwelberger H, Smit McBride Z, Kang H, Hershey J. Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae. Mol Cell Biol. 1991;11:3105-14 pubmed
    ..Two genes named TIF51A and TIF51B were cloned and sequenced...
  12. Gentz P, Blatch G, Dorrington R. Dimerization of the yeast eukaryotic translation initiation factor 5A requires hypusine and is RNA dependent. FEBS J. 2009;276:695-706 pubmed publisher
    ..We present a model of dimerization, based on the Neurospora crassa structural analogue, HEX-1. ..
  13. Reibarkh M, Yamamoto Y, Singh C, del Rio F, Fahmy A, Lee B, et al. Eukaryotic initiation factor (eIF) 1 carries two distinct eIF5-binding faces important for multifactor assembly and AUG selection. J Biol Chem. 2008;283:1094-103 pubmed
    ..Thus, eIF5 is an excellent candidate for the direct partner of eIF1-KH that mediates the critical link. The direct interaction at eIF1-KH also places eIF5 near the decoding site of the 40 S subunit. ..
  14. 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. ..
  15. Cano V, Medrano F, Park M, Valentini S. Evidence for conformational changes in the yeast deoxyhypusine hydroxylase Lia1 upon iron displacement from its active site. Amino Acids. 2010;38:479-90 pubmed publisher
    ..Our results demonstrate an essential structural role for iron binding in addition to its contribution to the catalysis of hypusine formation in the eIF-5A precursor. ..
  16. Rossi D, Galvão F, Bellato H, Boldrin P, Andrews B, Valentini S, et al. eIF5A has a function in the cotranslational translocation of proteins into the ER. Amino Acids. 2014;46:645-53 pubmed publisher
    ..These results link eIF5A function in translation with a role of SRP in the cell and may help explain the dual effects of eIF5A in differential and general translation. ..
  17. Li T, Belda Palazon B, Ferrando A, Alepuz P. Fertility and polarized cell growth depends on eIF5A for translation of polyproline-rich formins in Saccharomyces cerevisiae. Genetics. 2014;197:1191-200 pubmed publisher
    ..Since eIF5A and polyproline formins are conserved across species, our results also suggest that eIF5A-dependent translation of formins could regulate polarized growth in such processes as fertility and cancer in higher eukaryotes. ..
  18. Shin B, Katoh T, Gutierrez E, Kim J, Suga H, Dever T. Amino acid substrates impose polyamine, eIF5A, or hypusine requirement for peptide synthesis. Nucleic Acids Res. 2017;45:8392-8402 pubmed publisher
    ..Thus, we propose that the body of eIF5A functionally substitutes for polyamines to promote general protein synthesis and that the hypusine modification on eIF5A is critically important for poor substrates like proline. ..
  19. 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. ..
  20. Li X, Li Y, Arendt C, Hochstrasser M. Distinct Elements in the Proteasomal β5 Subunit Propeptide Required for Autocatalytic Processing and Proteasome Assembly. J Biol Chem. 2016;291:1991-2003 pubmed publisher
    ..Our results suggest that β7 insertion precedes half-mer dimerization, and the β7 tail and β5 propeptide have unequal roles in half-mer joining. ..
  21. Frigieri M, João Luiz M, Apponi L, Zanelli C, Valentini S. Synthetic lethality between eIF5A and Ypt1 reveals a connection between translation and the secretory pathway in yeast. Mol Genet Genomics. 2008;280:211-21 pubmed publisher
    ..In order to better understand the function of elF5A, a screen for synthetic lethal gene using the tif51A-3 mutant was carried out and a new mutation (G80D) was found in the essential gene YPT1, encoding a protein ..
  22. Galvão F, Rossi D, Silveira W, Valentini S, Zanelli C. The deoxyhypusine synthase mutant dys1-1 reveals the association of eIF5A and Asc1 with cell wall integrity. PLoS ONE. 2013;8:e60140 pubmed publisher
    ..The dys1-1 mutant was synthetically lethal in combination with asc1? and overexpression of TIF51A (eIF5A) or DYS1 is toxic for an asc1? strain...
  23. Barbosa N, Boldrin P, Rossi D, Yamamoto P, Watanabe T, Serrão V, et al. Mapping surface residues of eIF5A that are important for binding to the ribosome using alanine scanning mutagenesis. Amino Acids. 2016;48:2363-74 pubmed publisher
    ..We generated four new mutants of yeast eIF5A: tif51A-4, tif51A-6, tif51A-7 and tif51A-11, and complementation analysis revealed that tif51A-4 and tif51A-7 could not ..