The effect of hypusine modification on the intracellular localization of eIF5A

Biochemical and Biophysical Research Communications

Volumn 383, Issue 4, 2009, Pages 497-502

  Lee, Seung Bum ^a   Park, Jong Hwan ^a   Kaevel, Jörn ^a   Sramkova, Monika ^a   Weigert, Roberto ^a   Park, Myung Hee ^a  

^a NATIONAL INSTITUTE OF DENTAL AND CRANIOFACIAL RESEARCH   (United States)

Author keywords

Acetylation; Deoxyhypusine hydroxylase; Deoxyhypusine synthase; eIF5A; Hypusine; Nuclear export; Polyamine

Indexed keywords

DEOXYHYPUSINE HYDROXYLASE; DEOXYHYPUSINE SYNTHASE; HYPUSINE; INITIATION FACTOR 5A; MUTANT PROTEIN; OXYGENASE; POLYAMINE; UNCLASSIFIED DRUG;

ACETYLATION; ANIMAL CELL; ARTICLE; CELL NUCLEUS; CELLULAR DISTRIBUTION; CYTOPLASM; IMMUNOCYTOCHEMISTRY; MAMMAL CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN SYNTHESIS; SITE DIRECTED MUTAGENESIS;

ACETYLATION; CELL LINE; CYTOPLASM; HUMANS; LYSINE; MUTATION; PEPTIDE INITIATION FACTORS; PROTEIN PROCESSING, POST-TRANSLATIONAL; RNA-BINDING PROTEINS;

EUKARYOTA;

EID: 65449189139     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.04.049     Document Type: Article

References (22)

1. Park M.H. The post-translational synthesis of a polyamine-derived amino acid, hypusine, in the eukaryotic translation initiation factor 5A (eIF5A). J. Biochem. (Tokyo) 139 (2006) 161-169
2. Chen K.Y., and Liu A.Y. Biochemistry and function of hypusine formation on eukaryotic initiation factor 5A. Biol. Signals 6 (1997) 105-109
3. Zanelli C.F., and Valentini S.R. Is there a role for eIF5A in translation?. Amino Acids 33 (2007) 351-358
4. Abbruzzese A., Park M.H., and Folk J.E. Deoxyhypusine hydroxylase from rat testis. Partial purification and characterization. J. Biol. Chem. 261 (1986) 3085-3089
5. Schnier J., Schwelberger H.G., Smit-McBride Z., Kang H.A., and Hershey J.W. Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae. Mol. Cell Biol. 11 (1991) 3105-3114
6. Benne R., and Hershey J.W.B. The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes. J. Biol. Chem. 253 (1978) 3078-3087
7. Klier H., Csonga R., Joao H.C., Eckerskorn C., Auer M., Lottspeich F., and Eder J. Isolation and structural characterization of different isoforms of the hypusine-containing protein eIF-5A from HeLa cells. Biochemistry 34 (1995) 14693-14702
8. Park M.H. The essential role of hypusine in eukaryotic translation initiation factor 4D (eIF-4D). Purification of eIF-4D and its precursors and comparison of their activities. J. Biol. Chem. 264 (1989) 18531-18535
9. Smit-McBride Z., Schnier J., Kaufman R.J., and Hershey J.W. Protein synthesis initiation factor eIF-4D. Functional comparison of native and unhypusinated forms of the protein. J. Biol. Chem. 264 (1989) 18527-18530
10. Jao D.L., and Chen K.Y. Tandem affinity purification revealed the hypusine-dependent binding of eukaryotic initiation factor 5A to the translating 80S ribosomal complex. J. Cell. Biochem. 97 (2006) 583-598
11. Zanelli C.F., Maragno A.L., Gregio A.P., Komili S., Pandolfi J.R., Mestriner C.A., Lustri W.R., and Valentini S.R. eIF5A binds to translational machinery components and affects translation in yeast. Biochem. Biophys. Res. Commun. 348 (2006) 1358-1366
12. Gregio A.P.B., Cano V.P.S., Avaca J.S., Valentini S.R., and Zanelli C.F. eIF5A has a function in the elongation step of translation in yeast. Biochem. Biophys. Res. Commun. 380 (2009) 785-790
13. Ruhl M., Himmelspach M., Bahr G.M., Hammerschmid F., Jaksche H., Wolff B., Aschauer H., Farrington G.K., Probst H., Bevec D., et al. Eukaryotic initiation factor 5A is a cellular target of the human immunodeficiency virus type 1 Rev activation domain mediating trans-activation. J. Cell. Biol. 123 (1993) 1309-1320
14. Shi X.P., Yin K.C., Zimolo Z.A., Stern A.M., and Waxman L. The subcellular distribution of eukaryotic translation initiation factor, eIF-5A, in cultured cells. Exp. Cell Res. 225 (1996) 348-356
15. Jao L.-E.D., and Chen K.Y. Subcellular localization of the hypusine-containing eukaryotic initiation factor 5A by immunofluorescent staining and green fluorescent protein tagging. J. Cell. Biochem. 86 (2002) 590-600
16. Parreiras E.S.L.T., Gomes M.D., Oliveira E.B., and Costa-Neto C.M. The N-terminal region of eukaryotic translation initiation factor 5A signals to nuclear localization of the protein. Biochem. Biophys. Res. Commun. 362 (2007) 393-398
17. Li A.L., Li H.Y., Jin B.F., Ye Q.N., Zhou T., Yu X.D., Pan X., Man J.H., He K., Yu M., Hu M.R., Wang J., Yang S.C., Shen B.F., and Zhang X.M. A novel eIF5A complex functions as a regulator of p53 and p53-dependent apoptosis. J. Biol. Chem. 279 (2004) 49251-49258
18. Taylor C.A., Sun Z., Cliche D.O., Ming H., Eshaque B., Jin S., Hopkins M.T., Thai B., and Thompson J.E. Eukaryotic translation initiation factor 5A induces apoptosis in colon cancer cells and associates with the nucleus in response to tumour necrosis factor alpha signalling. Exp. Cell Res. 313 (2007) 437-449
19. Caraglia M., Marra M., Giuberti G., d'Alessandro A.M., Budillon A., del Prete S., Lentini A., Beninati S., and Abbruzzese A. The role of eukaryotic initiation factor 5A in the control of cell proliferation and apoptosis. Amino Acids 20 (2001) 91-104
20. Cano V.S., Jeon G.A., Johansson H.E., Henderson C.A., Park J.H., Valentini S.R., Hershey J.W., and Park M.H. Mutational analyses of human eIF5A-1-identification of amino acid residues critical for eIF5A activity and hypusine modification. FEBS J. 275 (2008) 44-58
21. Lipowsky G., Bischoff F.R., Schwarzmaier P., Kraft R., Kostka S., Hartmann E., Kutay U., and Görlich D. Exportin 4: a mediator of a novel nuclear export pathway in higher eukaryotes. EMBO J. 19 (2000) 4362-4371
22. Zender L., Xue W., Zuber J., Semighini C.P., Krasnitz A., Ma B., Zender P., Kubicka S., Luk J.M., Schirmacher P., McCombie W.R., Wigler M., Hicks J., Hannon G.J., Powers S., and Lowe S.W. An oncogenomics-based in vivo RNAi screen identifies tumor suppressors in liver cancer. Cell 135 (2008) 852-864