EIF5A dimerizes not only in vitro but also in vivo and its molecular envelope is similar to the EF-P monomer

Amino Acids

Volumn 44, Issue 2, 2013, Pages 631-644

  Dias, Camila Arnaldo Olhê ^a   Garcia, Wanius ^b   Zanelli, Cleslei Fernando ^a   Valentini, Sandro Roberto ^a  

^a SÃO PAULO STATE UNIVERSITY UNESP   (Brazil)

^b UNIVERSIDADE FEDERAL DO ABC   (Brazil)

Author keywords

Dimer; EF P; eIF5A; Hypusine; tRNA

Indexed keywords

DIMER; ELONGATION FACTOR; ELONGATION FACTOR P; HYPUSINE; INITIATION FACTOR 5A; MONOMER; OLIGOMER; TRANSFER RNA; UNCLASSIFIED DRUG;

ARTICLE; CELL NUCLEUS MEMBRANE; DIMERIZATION; GEL PERMEATION CHROMATOGRAPHY; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; PARTICLE SIZE; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN TERTIARY STRUCTURE; RADIATION SCATTERING; RIBOSOME; RNA STRUCTURE; STATIC ELECTRICITY; YEAST;

DIMERIZATION; HUMANS; MODELS, MOLECULAR; PEPTIDE ELONGATION FACTORS; PEPTIDE INITIATION FACTORS; RNA-BINDING PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EUKARYOTA;

EID: 84878364678     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-012-1387-7     Document Type: Article

References (54)

1. Bailly M, de Crécy-Lagard V (2010) Predicting the pathway involved in post-translational modification of elongation factor P in a subset of bacterial species. Biol Direct 5:3
2. Batista FA, Goto LS, Garcia W, de Moraes DI, de Oliveira Neto M, Polikarpov I, Cominetti MR, Selistre-de-Araújo HS, Beltramini LM, Araújo AP (2010) Camptosemin, a tetrameric lectin of Camptosema ellipticum: structural and functional analysis. Eur Biophys J 39(8):1193-1205
3. Benne R, Hershey JW (1978) The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes. J Biol Chem 253(9):3078-3087
4. Blaha G, Stanley RE, Steitz TA (2009) Formation of the first peptide bond: the structure of EF-P bound to the 70S ribosome. Science 325(5943):966-970
5. Chen KY, Liu AY (1997) Biochemistry and function of hypusine formation on eukaryotic initiation factor 5A. Biol Signals 6(3):105-109
6. Choi S, Choe J (2011) Crystal structure of elongation factor P from Pseudomonas aeruginosa at 1.75 A resolution. Proteins 79(5):1688-1693
7. Chung SI, Park MH, Folk JE, Lewis MS (1991) Eukaryotic initiation factor 5A: the molecular form of the hypusine-containing protein from human erythrocytes. Biochim Biophys Acta 1076(3):448-451
8. Delano WL (2002) The PyMOL molecular graphics system delano scientific
9. Dias CA, Cano VS, Rangel SM, Apponi LH, Frigieri MC, Muniz JR, Garcia W, Park MH, Garratt RC, Zanelli CF, Valentini SR (2008) 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 275(8):1874-1888
10. Dias CA, Gregio APB, Rossi D, Galvão FC, Watanabe TF, Park MH, Valentini SR, Zanelli CF (2012) eIF5A interacts functionally with eEF2. Amino Acids 42(2-3):697-702
11. Fischer H, de Oliveira Neto M, Napolitano HB, Polikarpov I, Craievich AF (2010) Determination of the molecular weight of proteins in solution from single small-angle X-ray scattering measurement on a relative scale. J Appl Cryst 43:101-109
12. Frigieri MC, Thompson GM, Pandolfi JR, Zanelli CF, Valentini SR (2007) Use of a synthetic lethal screen to identify genes related to TIF51A in Saccharomyces cerevisiae. Genet Mol Res 6(1):152-165
13. Frigieri MC, Joao Luiz MV, Apponi LH, Zanelli CF, Valentini SR (2008) Synthetic lethality between eIF5A and Ypt1 reveals a connection between translation and the secretory pathway in yeast. Mol Genet Genomics 280(3):211-221
14. Gentz PM, Blatch GL, Dorrington RA (2009) Dimerization of the yeast eukaryotic translation initiation factor 5A requires hypusine and is RNA dependent. FEBS J 276(3):695-706
15. Glick BR, Chladek S, Ganoza MC (1979) Peptide bond formation stimulated by protein synthesis factor EF-P depends on the aminoacyl moiety of the acceptor. Eur J Biochem/FEBS 97(1):23-28
16. Gough J, Karplus K, Hughey R, Chothia C (2001) Assignment of homology to genome sequences using a library of hidden Markov models that represent all proteins of known structure. J Mol Biol 313(4):903-919
17. Gregio AP, Cano VP, Avaca JS, Valentini SR, Zanelli CF (2009) eIF5A has a function in the elongation step of translation in yeast. Biochem Biophys Res Commun 380(4):785-790
18. Guinier A (1955) Small-angle scattering of X-rays. In: Fournet G, ed. John Wiley and Sons, New York
19. Hammerley AP (1997) FIT2D: An introduction and Overview. ESRF International Report
20. Hanawa-Suetsugu K, Sekine S, Sakai H, Hori-Takemoto C, Terada T, Unzai S, Tame JR, Kuramitsu S, Shirouzu M, Yokoyama S (2004) Crystal structure of elongation factor P from Thermus thermophilus HB8. Proc Nat Acad Sci USA 101(26):9595-9600
21. Henderson A, Hershey JW (2011) The role of eIF5A in protein synthesis. Cell Cycle 10(21):3617-3618
22. Hershey JW, Smit-McBride Z, Schnier J (1990) The role of mammalian initiation factor eIF-4D and its hypusine modification in translation. Biochim Biophys Acta 1050(1-3):160-162
23. Jao DL, Chen KY (2006) Tandem affinity purification revealed the hypusine-dependent binding of eukaryotic initiation factor 5A to the translating 80S ribosomal complex. J Cell Biochem 97(3):583-598
24. Kang HA, Hershey JW (1994) Effect of initiation factor eIF-5A depletion on protein synthesis and proliferation of Saccharomyces cerevisiae. J Biol Chem 269(6):3934-3940
25. Kellermann G, Vicentin F, Tamura E, Rocha M, Tolentino H, Barbosa A, Craievich A, Torriani I (1997) The small-angle X-ray scattering beamline of the Brazilian Synchrotron Light Laboratory. J Appl Crystallogr 30(2):880-883
26. Kemper WM, Berry KW, Merrick WC (1976) Purification and properties of rabbit reticulocyte protein synthesis initiation factors M2Balpha and M2Bbeta. J Biol Chem 251(18):5551-5557
27. Konarev PV (2006) ATSAS 2.1, a program package for small-angle scattering data analysis. J Appl Cryst 39:277-286
28. Kozin MB, Svergun DI (2001) Automated matching of high- and low-resolution structural models. J Appl Crystallogr 34:33-41
29. Lancaster L, Kiel MC, Kaji A, Noller HF (2002) Orientation of ribosome recycling factor in the ribosome from directed hydroxyl radical probing. Cell 111(1):129-140
30. Nakamura Y, Ito K (2003) Making sense of mimic in translation termination. Trends Biochem Sci 28(2):99-105
31. Navarre WW, Zou SB, Roy H, Xie JL, Savchenko A, Singer A, Edvokimova E, Prost LR, Kumar R, Ibba M, Fang FC (2010) PoxA, yjeK, and elongation factor P coordinately modulate virulence and drug resistance in Salmonella enterica. Mol Cell 39(2):209-221
32. Orthaber D, Bergmann A, Glatter O (2000) SAXS experiments on absolute scale with Kratky systems using water as a secondary standard. J Appl Cryst 33:218-225
33. Park MH, Wolff EC, Folk JE (1993) Is hypusine essential for eukaryotic cell proliferation? Trends Biochem Sci 18(12):475-479
34. Park MH, Lee YB, Joe YA (1997) Hypusine is essential for eukaryotic cell proliferation. Biol Signals 6(3):115-123
35. Park MH, Nishimura K, Zanelli CF, Valentini SR (2010) Functional significance of eIF5A and its hypusine modification in eukaryotes. Amino Acids 38(2):491-500
36. Park JH, Dias CA, Lee SB, Valentini SR, Sokabe M, Fraser CS, Park MH (2011) Production of active recombinant eIF5A: reconstitution in E. coli of eukaryotic hypusine modification of eIF5A by its coexpression with modifying enzymes. Protein Eng Des Sel 24(3):301-309
37. Park JH, Johansson HE, Aoki H, Huang BX, Kim HY, Ganoza MC, Park MH (2012) Post-translational modification by β-lysylation is required for activity of Escherichia coli elongation factor P (EF-P). J Biol Chem 287(4):2579-2590
38. Petoukhov MV, Svergun DI (2003) New methods for domain structure determination of proteins from solution scattering data. J Appl Crystallogr 36:540-544
39. Prinz B, Schultchen J, Rydzewski R, Holz C, Boettner M, Stahl U, Lang C (2004) Establishing a versatile fermentation and purification procedure for human proteins expressed in the yeasts Saccharomyces cerevisiae and Pichia pastoris for structural genomics. J Struct Funct Genomics 5(1-2):29-44
40. Roy H, Zou SB, Bullwinkle TJ, Wolfe BS, Gilreath MS, Forsyth CJ, Navarre WW, Ibba M (2011) The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-beta-lysine. Nat Chem Biol 7(10):667-669
41. Saini P, Eyler DE, Green R, Dever TE (2009) Hypusine-containing protein eIF5A promotes translation elongation. Nature 459(7243):118-121
42. Schnier J, Schwelberger HG, Smit-McBride Z, Kang HA, Hershey JW (1991) Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae. Mol Cell Biol 11(6):3105-3114
43. Svergun D (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J Appl Cryst 25:495-503
44. Svergun DI (1999) Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys J 76(6):2879-2886
45. Svergun D, Petoukhov Koch M (2001) Determination of domain structure of proteins from X-ray solution scattering. Biophys J 80:2946-2953
46. Svergun DI, Semenyuk AV, Feigin LA (1988) Small-angle-scattering-data treatment by the regularization method. Acta Crystallogr A 44:244-250
47. Tong Y, Park I, Hong BS, Nedyalkova L, Tempel W, Park HW (2009) Crystal structure of human eIF5A1: insight into functional similarity of human eIF5A1 and eIF5A2. Proteins 75(4):1040-1045
48. Vestergaard B, Van LB, Andersen GR, Nyborg J, Buckingham RH, Kjeldgaard M (2001) Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1. Mol Cell 8(6):1375-1382
49. William KR, Lopresti M, Stone K (1997) Internal protein sequencing of SDS-PAGE separated proteins: optimization of an in-gel digest protocol. In: Marshak D (ed) Techniques VIII. Academic Press, San Diego, pp 79-90
50. Xu A, Chen KY (2001) Hypusine is required for a sequence-specific interaction of eukaryotic initiation factor 5A with post systematic evolution of ligands by exponential enrichment RNA. J Biol Chem 276(4):2555-2561
51. Xu A, Jao DL, Chen KY (2004) Identification of mRNA that binds to eukaryotic initiation factor 5A by affinity co-purification and differential display. Biochem J 384(Pt 3):585-590
52. Yanagisawa T, Sumida T, Ishii R, Takemoto C, Yokoyama S (2010) A paralog of lysyl-tRNA synthetase aminoacylates a conserved lysine residue in translation elongation factor P. Nat Struct Mol Biol 17(9):1136-1143
53. Zanelli CF, Valentini SR (2005) Pkc1 acts through Zds1 and Gic1 to suppress growth and cell polarity defects of a yeast eIF5A mutant. Genetics 171(4):1571-1581
54. Zanelli CF, Maragno AL, Gregio AP, Komili S, Pandolfi JR, Mestriner CA, Lustri WR, Valentini SR (2006) eIF5A binds to translational machinery components and affects translation in yeast. Biochem Biophys Res Commun 348(4):1358-1366