Mutational analysis of mammalian translation initiation factor 5 (eIF5): Role of interaction between the β subunit of eIF2 and eIF5 in eIF5 function in vitro and in vivo

Molecular and Cellular Biology

Volumn 20, Issue 11, 2000, Pages 3942-3950

  Das, Supratik ^a   Maitra, Umadas ^a,b  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^b YESHIVA UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BETA CHAIN; CELL GROWTH; CELL VIABILITY; CHROMOSOME; GENE MUTATION; HYDROLYSIS; MAMMAL; MUTAGENESIS; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE; TRANSLATION INITIATION; YEAST;

ALANINE; AMINO ACID SUBSTITUTION; ANIMALS; ARTEMIA; EUKARYOTIC INITIATION FACTOR-2; EUKARYOTIC INITIATION FACTOR-5; FUNGAL PROTEINS; GUANOSINE TRIPHOSPHATE; HYDROLYSIS; MAMMALS; MUTAGENESIS; NUCLEAR PROTEINS; PEPTIDE INITIATION FACTORS; PROTEIN BIOSYNTHESIS; RABBITS; RATS; RECOMBINANT FUSION PROTEINS; RIBOSOMAL PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EUKARYOTA; MAMMALIA; SACCHAROMYCES CEREVISIAE;

EID: 0034122792     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.20.11.3942-3950.2000     Document Type: Article

References (26)

1. Asano, K., T. Krishnamoorthy, L. Phan, G. D. Pavitt, and A. G. Hinnebusch. 1999. Conserved bipartite motifs in yeast eIF5 and eIF2Bε, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2. EMBO J. 18:1673-1688.
2. Bandyopadhyay, A., and U. Maitra. 1999. Cloning and characterization of the p42 subunit of mammalian translation initiation factor 3 (eIF3): demonstration that eIF3 interacts with eIF5 in mammalian cells. Nucleic Acids Res. 27:1331-1337.
3. Bourne, H. R., D. A. Sanders, and F. McCormick. 1991. The GTPase super-family: conserved structure and molecular mechanism. Nature 349:117-127.
4. Chakrabarti, A., and U. Maitra. 1991. Function of eukaryotic initiation factor 5 in the formation of an 80S ribosomal polypeptide chain initiation complex. J. Biol. Chem. 266:14039-14045.
5. Chakravarti, D., T. Maiti, and U. Maitra. 1993. Isolation and immunochemical characterization of eukaryotic translation initiation factor 5 from Sacckaromyces cerevisiae. J. Biol. Chem. 268:5754-5762.
6. Chakravarti, D., and U. Maitra. 1993. Eukaryotic initiation factor 5 from Saccharomyces cerevisiae. J. Biol. Chem. 268:10524-10533.
7. Chaudhuri, J., K. Das, and U. Maitra. 1994. Purification and characterization of bacterially expressed mammalian translation initiation factor 5 (eIF5): demonstration that eIF5 forms a specific complex with eIF2. Biochemistry 33:4794-4799.
8. Chaudhuri, J., K. Si, and U. Maitra. 1997. Function of eukaiyotic translation initiation factor 1A (eIF1A) (formerly called eIF-4C) in initiation of protein synthesis. J. Biol. Chem. 272:7883-7891.
9. Chevesich, J., J. Chaudhuri, and U. Maitra. 1993. Characterization of mammalian initiation factor 5 (eIF5). J. Biol. Chem. 268:20659-20667.
10. Das, K., J. Chevesich, and U. Maitra. 1993. Molecular cloning and expression of cDNA for mammalian translation initiation factor 5. Proc. Natl. Acad. Sci. USA 90:3058-3062.
11. Das, S., T. Maiti, K. Das, and U. Maitra. 1997. Specific interaction of eukaryotic translation initiation factor 5 (eIF5) with the β subunit of eIF2. J. Biol. Chem. 272:31712-31718.
12. Ghosh, S., J. Chevesich, and U. Maitra. 1989. Further characterization of eukaryotic initiation factor 5 from rabbit reticulocytes. Immunochemical characterization and phosphorylation by casein kinase II. J. Biol. Chem. 264:5134-5140.
13. Gu, G., R. P. Moerschell, F. Sherman, and D. S. Goldfarb. 1992. N1P1, a gene required for nuclear transport in yeast. Proc. Natl. Acad. Sci. USA 89:10355-10359.
14. Hannig, E. M., A. M. Cigan, B. A. Freeman, and T. G. Kinzy. 1993. GCD11. a negative regulator of GCN4 expression, encodes the γ subunit of eIF2 in Saccharomyces cerevisiae. Mol. Cell. Biol. 13:506-520.
15. Huang, H.-K., H. Yoon, E. M. Hannig, and T. F. Donahue. 1997. GTP hydrolysis controls stringent selection of the AUG start codon during translation initiation in Saccharomyces cerevisiae. Genes Dev. 11:2396-2413.
16. Kozak, M. 1999. Initiation of translation in prokaryotes and eukaryotes. Gene 234:187-208.
17. Maiti, T., and U. Maitra. 1997. Characterization of translation initiation factor 5 (eIF5) from Saccharomyces cerevisiae. Functional homology with mammalian eIF5 and the effect of depletion of eIF5 on protein synthesis in vivo and in vitro. J. Biol. Chem. 272:18333-18340.
18. Maitra, U., E. A. Stringer, and A. Chaudhuri. 1982. Initiation factors in protein biosynthesis. Annu. Rev. Biochem. 51:869-900.
19. Merrick, W. C., and J. W. B. Hershey. 1996. The pathway and mechanism of eukaryotic protein synthesis, p. 31-69. In J. W. B. Hershey, M. B. Mathews, and N. Sonenberg, (ed.), Translational control. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
20. Phan, L., X. Zhang, K. Asano, J. Anderson, H. P. Vornlocher, J. R. Greenberg, J. Qin, and A. G. Hinnebusch. 1998. Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5. Mol. Cell. Biol. 18:4935-4946.
21. r = 62,000. J. Biol. Chem. 260:2132-2139.
22. Rose, M. D., F. Winston, and P. Hieter. 1989. Methods in yeast genetics: a laboratory course manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N. Y.
23. Sachs, A. B., and J. A. Deardorff. 1992. Translation initiation requires the PAB-dependent poly(A) ribonuclease in yeast. Cell 70:961-973.
24. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
25. Scheffzek, K., M. R. Ahmadian, and A. Wittinghofer. 1998. GTPase-activating proteins: helping hands to complement an active site. Trends Biochem. Sci. 23:257-262.
26. Si, K., K. Das, and U. Maitra. 1996. Characterization of multiple mRNAs that encode mammalian translation initiation factor 5 (eIF5). J. Biol. Chem. 271:16934-16938.