Kinetic analysis of the interaction of guanine nucleotides with eukaryotic translation initiation factor eIF5B

Biochemistry

Volumn 46, Issue 10, 2007, Pages 2622-2629

  Pisareva, Vera P ^a   Hellen, Christopher U T ^a   Pestova, Tatyana V ^a,b  

^a SUNY DOWNSTATE MEDICAL CENTER   (United States)

^b MOSCOW STATE UNIVERSITY   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEOTIDE EXCHANGE FACTOR; RIBOSOME; TRIPHOSPHATE MOIETY;

DISSOCIATION; ENZYME KINETICS; GROWTH KINETICS; HORMONES; HYDROLYSIS;

NUCLEOTIDES;

GUANINE NUCLEOTIDE; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; GUANYLYLIMIDODIPHOSPHATE; INITIATION FACTOR 5; INITIATION FACTOR 5B; RIBOSOME RNA; RNA 40S; RNA 60S; RNA 80S; UNCLASSIFIED DRUG;

ANALYTIC METHOD; ARTICLE; BINDING AFFINITY; DISSOCIATION; ENZYME ACTIVITY; FLUORESCENCE; FLUORESCENT STOPPED FLOW TECHNIQUE; HYDROLYSIS; KINETICS; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FUNCTION; REACTION ANALYSIS; TRANSLATION INITIATION;

ANIMALS; EUKARYOTIC INITIATION FACTORS; GUANINE NUCLEOTIDES; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; KINETICS; RABBITS;

EUKARYOTA;

EID: 33947211185     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi062134g     Document Type: Article

References (34)

1. Pestova, T. V., Kolupaeva, V. G., Lomakin, I. B., Pilipenko, E. V., Shatsky, I. N., Agol, V. I., and Hellen, C. U. T. (2001) Molecular mechanisms of translation initiation in eukaryotes, Proc. Natl. Acad. Sci. U.S.A. 98, 7029-7036.
2. Das, S., and Maitra, U. (2001) Functional significance and mechanism of eIF5-promoted GTP hydrolysis in eukaryotic translation initiation, Prog. Nucleic Acid Res. Mol. Biol. 70, 207-231.
3. Unbehaun, A., Borukhov, S. I., Hellen, C. U. T., and Pestova, T. V. (2003) Release of initiation factors from 48S complexes during ribosomal subunit joining and the link between establishment of codon-anticodon base-pairing and hydrolysis of eIF2-bound GTP, Genes Dev. 18, 3078-3093.
4. Algire, M. A., Maag, D., and Lorsch, J. R. (2005) Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation, Mol. Cell 20, 251-262.
5. Kapp, L. D., and Lorsch, J. R. (2004) GTP-dependent recognition of the methionine moiety on initiator tRNA by translation factor eIF2, J. Mol. Biol. 335, 923-936.
6. Pisarev, A. V., Kolupaeva, V. G., Pisareva, V. P., Merrick, W. C., Hellen, C. U. T., and Pestova, T. V. (2006) Specific functional interactions of nucleotides at key -3 and +4 positions flanking the initiation codon with components of the mammalian 48S translation initiation complex, Genes Dev. 20, 624-636.
7. Pestova, T. V., Lomakin, I. B., Lee, J. H., Choi, S. K., Dever, T. E., and Hellen, C. U. T. (2000) The joining of ribosomal subunits in eukaryotes requires eIF5B, Nature 403, 332-335.
8. Lee, J. H., Choi, S. K., Roll-Mecak, A., Burley, S. K., and Dever, T. E. (1999) Universal conservation in translation initiation revealed by human and archaeal homologs of bacterial translation initiation factor IF2, Proc. Natl. Acad. Sci. U.S.A. 96, 4342-4347.
9. Kolakofsky, D., Dewey, K. F., Hershey, J. W. B., and Thach, R. E. (1968) Guanosine 5′-triphosphatase activity of initiation factor f2, Proc. Natl. Acad. Sci. U.S.A. 61, 1066-1070.
10. Pestova, T. V., Dever, T. E., and Hellen, C. U. T. (2000) Ribosomal subunit joining, in Translational Control of Gene Expression (Sonenberg, N., Hershey, J. W. B., and Mathews, M. B., Eds.) pp 425-445, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
11. Laalami, S., Timofeev, A. V., Putzer, H., Leautey, J., and Grunberg-Manago, M. (1994) In vivo study of engineered G-domain mutants of Escherichia coli translation initiation factor IF2, Mol Microbiol. 11, 293-302.
12. Luchin, S., Putzer, H., Hershey, J. W., Cenatiempo, Y., Grunberg-Manago, M., and Lalaami, S. (1999) In vitro study of two dominant inhibitory GTPase mutants of Escherichia coli translation initiation factor 2. Direct evidence that GTP hydrolysis is necessary for factor recycling, J. Biol. Chem. 274, 6074-6079.
13. Laursen, B. S., Siwanowicz, I., Larigauderie, G., Hedegaard, J., Ito, K., Nakamura, Y., Kenney, J. M., Mortensen, K. K., and Sperling-Petersen, H. U. (2003) Characterization of mutations in the GTP-binding domain of IF22 resulting in cold-sensitive growth of Escherichia coli, J. Mol. Biol. 326, 543-551.
14. Lee, J. H., Pestova, T. V., Shin, B. S., Cao, C., Choi, S. K., and Dever, T. E. (2002) Initiation factor eIF5B catalyzes second GTP-dependent step in eukaryotic translation initiation, Proc. Natl. Acad. Sci. U.S.A. 99, 16689-16694.
15. Roll-Mecak, A., Cao, C., Dever, T. E., and Burley, S. K. (2000) X-Ray structures of the universal translation initiation factor IF2/ eIF5B: conformational changes on GDP and GTP binding, Cell 103, 781-792.
16. Kubarenko, A. V., Sergiev, P. V., and Rodnina, M. V. (2005) GTPases of the translational apparatus, Mol. Biol. (Moscow) 39, 746-761.
17. 2+ and guaninine nuclotide exchange factor on the binding of guanine nucleotides to eukaryotic initiation factor 2, J. Biol. Chem. 263, 5519-5525.
18. Gromadski, K. B., Wieden, H. J., and Rodnina, M. V. (2002) Kinetic mechanism of elongation factor Ts-catalyzed nucleotide exchange in elongation factor Tu, Biochemistry 41, 162-169.
19. Gill, S. C., and von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data, Anal. Biochem. 182, 319-326.
20. Hemsath, L., and Ahmadian, M. R. (2005) Fluorescence approaches for monitoring interactions of Rho GTPases with nucleotides, regulators, and effectors, Methods 37, 173-178.
21. John, J., Sohmen, R., Feuerstein, J., Linke, R., Wittinghofer, A., and Goody, R. S. (1990) Kinetics of interaction of nucleotides with nucleotide-free H-ras p21, Biochemistry 29, 6058-6065.
22. Rodnina, M. V., Fricke, R., Kuhn, L., and Wintermeyer, W. (1995) Codon-dependent conformational change of elongation factor Tu preceding GTP hydrolysis on the ribosome, EMBO J. 14, 2613-2619.
23. Rensland, H., Lautwein, A., Wittinghofer, A., and Goody, R. S. (1991) Is there a rate-limiting step before GTP cleavage by H-ras p21?, Biochemistry 30, 11181-11185.
24. Traut, T. W. (1994) Physiological concentrations of purines and pyrimidines, Mol. Cell. Biochem. 140, 1-22.
25. Pon, C. L., Paci, M., Pawlik, R. T., and Gualerzi, C. O. (1985) Structure-function relationship in Escherichia coli initiation factors. Biochemical and biophysical characterization of the interaction between IF-2 and guanosine nucleotides, J. Biol. Chem. 260, 8918-8924.
26. Milon, P., Tischenko, E., Tomsic, J., Caserta, E., Folkers, G., La Teana, A., Rodnina, M. V., Pon, C. L., Boelens, R., and Gualerzi, C. O. (2006) The nucleotide-binding site of bacterial translation initiation factor 2 (IF2) as a metabolic sensor, Proc. Natl. Acad. Sci. U.S.A. 103, 13962-13967.
27. Antoun, A., Pavlov, M. Y., Andersson, K., Tenson, T., and Ehrenberg, M. (2003) The roles of initiation factor 2 and guanosine triphosphate in initiation of protein synthesis, EMBO J. 22, 5593-5601.
28. Zavialov, A. V., Buckingham, R. H., and Ehrenberg, M. (2001) A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3, Cell 107, 115-124.
29. Nurten, R., and Bermek, E. (1980) Interactions of elongation factor 2 (EF-2) with guanine nucleotides and ribosomes. Binding of periodate-oxidized guanine nucleotides to EF-2, Eur. J. Biochem. 103, 551-555.
30. Raimo, G., Masullo, M., and Bocchini, V. (1995) Studies on the polypeptide elongation factor 2 from Sulfolobus solfataricus. Interaction with guanosine nucleotides and GTPase activity stimulated by ribosomes, J. Biol. Chem. 270, 21082-21085.
31. Baca, O. G., Rohrbach, M. S., and Bodley, J. W. (1976) Equilibrium measurements of the interactions of guanine nucleotides with Escherichia coli elongation factor G and the ribosome, Biochemistry 15, 4570-4574.
32. Wilden, B., Savlesbergh, A., Rodnina, M. V., and Wintermeyer, W. (2006) Role and timing of GTP binding and hydrolysis during EF-G-dependent tRNA translocation on the ribosome, Proc. Natl. Acad. Sci. U.S.A. 103, 13670-13675.
33. Hauryliuk, V., Zavialov, A., Kisselev, L., and Ehrenberg, M. (2006) Class-1 release factor eRF1 promotes GTP binding by class-2 release factor eRF3, Biochimie 88, 747-457.
34. Vetter, I. R., and Wittinghofer, A. (2001) The guanine nucleotide-binding switch in three dimensions, Science 294, 1299-1304.