Effects of poly(A)-binding protein on the interactions of translation initiation factor eIF4F and eIF4F·4B with internal ribosome entry site (IRES) of tobacco etch virus RNA

Biochimica et Biophysica Acta - Gene Regulatory Mechanisms

Volumn 1779, Issue 10, 2008, Pages 622-627

  Khan, Mateen A ^a   Yumak, Hasan ^a   Gallie, Daniel R ^b   Goss, Dixie J ^a  

^a CITY UNIVERSITY OF NEW YORK   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

eIF's; Equilibrium; Fluorescence anisotropy; IRES; TEV; Thermodynamic

Indexed keywords

INITIATION FACTOR; INITIATION FACTOR 4B; INITIATION FACTOR 4F; POLYADENYLIC ACID BINDING PROTEIN;

ANISOTROPY; ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; ENTROPY; FLUORESCENCE; INTERNAL RIBOSOME ENTRY SITE; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; RNA BINDING; RNA VIRUS; TOBACCO; TRANSLATION INITIATION;

BINDING SITES; EUKARYOTIC INITIATION FACTOR-4F; EUKARYOTIC INITIATION FACTORS; FLUORESCENCE POLARIZATION; HYDROPHOBICITY; PICORNAVIRIDAE; POLY(A)-BINDING PROTEINS; PROTEIN BINDING; RIBOSOMES; RNA, VIRAL; TEMPERATURE; TOBACCO; TRITICUM;

EUKARYOTA; TOBACCO ETCH VIRUS; TRITICUM AESTIVUM;

EID: 52049092086     PISSN: 18749399     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagrm.2008.07.004     Document Type: Article

References (51)

1. Jackson R.J., and Standart N. Do the poly(A) tail and 3′ untranslated region control mRNA translation?. Cell 62 (1990) 15-24
2. Munroe D., and Jacobson A. mRNA poly(A) tail, a 3′ enhancer of translational initiation. Mol. Cell. Biol. 10 (1990) 3441-3455
3. Munroe D., and Jacobson A. Tales of poly(A): a review. Gene 91 (1990) 151-158
4. Bernstein P., and Ross J. Poly(A), poly(A) binding protein and the regulation of mRNA stability. Trends Biochem. Sci. 14 (1989) 373-377
5. Sonenberg N. Cap binding proteins of eukaryotic messenger RNA: functions in initiation and control of translation. Prog. Nucl. Acid. Res. and Mol. Biol. 35 (1988) 173-207
6. Rhoads R.E. Cap recognition and the entry of mRNA into the protein synthesis initiation cycle. Trends Biochem. Sci. 13 (1988) 52-56
7. Gallie D.R., and Tanguay R. Poly(A) binds to initiation factors and increases cap-dependent translation in vitro. J. Biol. Chem. 269 (1994) 17166-17173
8. Tarun Jr. S.Z., and Sachs A.B. Association of the yeast poly(A) tail binding protein with translation initiation factor eIF-4G. EMBO J. 15 (1996) 7168-7177
9. Le H., Tanguay R.L., Balasta M.L., Wei C.C., Browning K.S., Metz A.M., Goss D.J., and Gallie D.R. The translation initiation factors eIF-iso4G and eIF4B interact with the poly(A)-binding protein and increase its RNA binding affinity. J. Biol. Chem. 272 (1997) 16247-16255
10. Merrick W.C. Mechanism and regulation of eukaryotic protein synthesis. Microbiol. Rev. 56 (1992) 291-315
11. Gingras A.C., Raught B., and Sonenberg N. eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Annu. Rev. Biochem. 68 (1999) 913-963
12. Hershey J.W.B., and Merrick W.C. The Pathway and Mechanism of Initiation of Protein Synthesis, in Translational Control of Gene Expression (2000), Cold Spring Harbor Laboratory Press, Plainview, NY
13. Morley S.J. The Regulation of eIF4F During Cell Growth and Cell Death, Signaling Pathway for Translation (2001), Springer-Verlag, Berlin
14. Gallie D.R. A tale of two termini: a functional interaction between the termini of an mRNA is a prerequisite for efficient translation initiation. Gene 216 (1998) 1-11
15. Wells S.E., Hillner P.E., Vale R.D., and Sachs A.B. Circularization of mRNA by eukaryotic translation initiation factors. Mol. Cell 2 (1998) 135-140
16. Imataka H., Gradi A., and Sonenberg N. A newly identified N-terminal amino acid sequence of human eIF4G binds poly(a)-binding protein and functions in poly(A)-dependent translation. EMBO J. 17 (1998) 7480-7489
17. Wei C.-C., Balasta M.L., Ren J., and Goss D.J. Wheat germ poly(A) binding protein enhances the binding affinity of eukaryotic initiation factor 4F and (iso)4F for cap analogs. Biochemistry 37 (1998) 1910-1916
18. Le H., Browning K.S., and Gallie D.R. The phosphorylation state of poly(A)-binding protein specifies its binding to poly(A) RNA and its interaction with eukaryotic initiation factor (eIF) 4F, eIFiso4F, and eIF4B. J. Biol. Chem. 275 (2000) 17452-17462
19. Lawson T.G., Lee K.A., Maimone M.M., Abramson R.D., Dever T.E., Merrick W.C., and Thach R.E. Dissociation of double-stranded polynucleotide helical structures by eukaryotic initiation factors, as revealed by a novel assay. Biochemistry 28 (1989) 4729-4734
20. Milburn S.C., Hershey J.W., Davies M.V., Kelleher K., and Kaufman R.J. Cloning and expression of eukaryotic initiation factor 4B cDNA: sequence determination identifies a common RNA recognition motif. EMBO J. 9 (1990) 2783-2790
21. Rozen F., Edery I., Meerovitch K., Dever T.E., Merrick W.C., and Sonenberg N. Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4F. Mol. Cell Biol. 10 (1990) 1134-1144
22. Jaramillo M., Dever T.E., Merrick W.C., and Sonenberg N. RNA unwinding in translation: Assembly of helicase complex intermediates comprising eukaryotic initiation factors eIF4F and eIF4B. Mol. Cell Biol. 11 (1991) 5992-5997
23. Altmann M., Muller P.P., Wittmer B., Ruchti F., Lanker S., and Trachsel H. A Saccharomyces cerevisiae homologue of mammalian translation initiation factor 4B contributes to RNA helicase activity. EMBO J. 12 (1993) 3997-4003
24. Methot N., Pause A., Hershey J.W., and Sonenberg N. The translation initiation factor eIF-4B contains an RNA-binding region that is distinct and independent from its ribonucleoprotein consensus sequence. Mol. Cell Biol. 14 (1994) 2307-2316
25. Merrick W.C. Eukaryotic protein synthesis: an in vitro analysis. Biochimie 76 (1994) 822-830
26. Rogers G.W., Richter N.J., and Merrick W.C. Biochemical and kinetic characterization of the RNA helicase activity of eukaryotic initiation factor 4A. J. Biol. Chem 274 (1999) 12236-12244
27. Rogers Jr. G.W., Richter N.J., Lima W.F., and Merrick W.C. Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F. J. Biol. Chem. 276 (2001) 30914-30922
28. Lax S., Fritz W., Browning K., and Ravel J. Isolation and characterization of factors from wheat germ that exhibit eukaryotic initiation factor 4B activity and overcome 7-methylguanosine 5′-triphosphate inhibition of polypeptide synthesis. Proc. Natl. Acad. Sci. U. S. A 82 (1985) 330-333
29. Lax S.R., Browning K.S., Maia D.M., and Ravel J.M. ATPase activities of wheat germ initiation factors 4A, 4B, and 4F. J. Biol. Chem. 261 (1986) 15632-15636
30. Browning K.S., Lax S.R., and Ravel J.M. Identification of two messenger RNA cap binding proteins in wheat germ. Evidence that the 28-kDa subunit of eIF-4B and the 26-kDa subunit of eIF-4F are antigenically distinct polypeptides. J. Biol. Chem 262 (1987) 11228-11232
31. Browning K.S., Fletcher L., Lax S.R., and Ravel J.M. Evidence that the 59-kDa protein synthesis initiation factor from wheat germ is functionally similar to the 80-kDa initiation factor 4B from mammalian cells. J. Biol. Chem. 264 (1989) 8491-8494
32. Carrington J.C., and Freed D.D. Cap-independent enhancement of translation by a plant potyvirus 5′ nontranslated region. J. Virol. 64 (1990) 1590-1597
33. Gallie D.R., and Browning K.S. eIF4G functionally differs from eIFiso4G in promoting internal initiation, cap-independent translation, and translation of structured mRNAs. J. Biol. Chem. 276 (2001) 36951-36960
34. Gallie D., Tanguay R., and Leathers V. The tobacco etch viral 5′ leader and poly(A) tail are synergistic regulators of translation. Gene 165 (1995) 233-238
35. Gallie D.R. Cap-independent translation conferred by the 5′ leader of tobacco etch virus is eukaryotic initiation factor 4G dependent. J. Virol. 75 (2001) 12141-12152
36. Ray S., Yumak H., Domashevskiy A., Khan M.A., Gallie D.R., and Goss D.J. Tobacco etch virus mrna preferentially binds wheat germ eukaryotic initiation factor (eIF) 4G rather than eIFiso4G. J. Biol. Chem. 281 (2006) 35826-35834
37. Tarun Jr. S.Z., and Sachs A.B. A common function for mRNA 5′ and 3′ ends in translation initiation in yeast. Genes. Dev. 9 (1995) 2997-3007
38. Zeenko V., and Gallie D.R. Cap-independent translation of tobacco etch virus is conferred by an RNA pseudoknot in the 5′-leader. J. Biol. Chem. 280 (2005) 26813-26824
39. Lax S.R., Lauer S.J., Browning K.S., and Ravel J.M. Purification and properties of protein synthesis initiation and elongation factors from wheat germ. Methods Enzymol 118 (1986) 109-128
40. van Heerden A., and Browning K.S. Expression in Escherichia coli of the two subunits of the isozyme form of wheat germ protein synthesis initiation factor 4F. Purification of the subunits and formation of an enzymatically active complex. J. Biol. Chem. 269 (1994) 17454-17457
41. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 72 (1976) 248-254
42. Kohler J.J., and Schepartz A. Kinetic studies of Fos.Jun.DNA complex formation: DNA binding prior to dimerization. Biochemistry. 40 (2001) 130-142
43. Zitzewitz J.A., Bilsel O., Luo J., Jones B.E., and Matthews C.R. Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy. Biochemistry 34 (1995) 12812-12819
44. Scatchard G. The attraction of proteins for small molecules and ions. Ann. N.Y. Acad. Sci. 51 (1949) 660-672
45. Khan M.A., Kumar Y., and Tayyab S. Bilirubin binding properties of pigeon serum albumin and its comparison with human serum albumin. Int. J. Biol. Macromol. 30 (2002) 171-178
46. Tayyab S., Khan N.J., Khan M.A., and Kumar Y. Behavior of various mammalian albumins towards bilirubin binding and photochemical properties of different bilirubin-albumin complexes. Int. J. Biol. Macromol. 31 (2003) 187-193
47. Khan M.A., Miyoshi H., Gallie D.R., and Goss D.J. Potyvirus genome-linked protein, VPg, directly affects wheat germ in vitro translation: interactions with translation initiation factors eIF4F and eIFiso4F. J. Biol. Chem. 283 (2008) 1340-1349
48. Carberry S.E., and Goss D.J. Wheat germ initiation factors 4F and (iso)4F interact differently with oligoribonucleotide analogues of rabbit alpha-globin mRNA. Biochemistry 30 (1991) 4542-4545
49. Carberry S.E., Darzynkiewicz E., and Goss D.J. A comparison of the binding of methylated cap analogues to wheat germ protein synthesis initiation factors 4F and (iso)4F. Biochemistry 30 (1991) 1624-1627
50. Poncet D., Laurent S., and Cohen J. Four nucleotides are the minimal requirement for RNA recognition by rotavirus non-structural protein NSP3. EMBO J. 13 (1994) 4165-4173
51. Khan M.A., and Goss D.J. Translation initiation factor (eIF) 4B affects the rates of binding of the mRNA m7G cap analogue to wheat germ eIFiso4F and eIFiso4F·PABP. Biochemistry 44 (2005) 4510-4516