Identification of a regulatory subcomplex in the guanine nucleotide exchange factor eIF2B that mediates inhibition by phosphorylated eIF2

Molecular and Cellular Biology

Volumn 16, Issue 11, 1996, Pages 6603-6616

  Yang, Weimin ^a   Hinnebusch, Alan G ^a  

^a EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH AND HUMAN DEVELOPMENT   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE EXCHANGE FACTOR; INITIATION FACTOR 2;

ARTICLE; CARBOXY TERMINAL SEQUENCE; NONHUMAN; PHOSPHORYLATION; POINT MUTATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN SYNTHESIS; REGULATORY MECHANISM; TRANSLATION INITIATION;

EUKARYOTA;

EID: 0029805459     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.16.11.6603     Document Type: Article

References (36)

1. Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
2. Burnette, W. 1981. "Western blotting": clectrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem. 112:195-203.
3. Bushman, J. L., A. I. Asuru, R. L. Matts, and A. U. Hinnebusch. 1993. Evidence that GCD6 and GCD7, translational regulators of GCN4, are subunits of the guanine nucleotide exchange factor for eIF-2 in Saccharomyces cerevisiae. Mol. Cell. Biol. 13:1920-1932.
4. Bushman, J. L., M. Foiani, A. M. Cigan, C. J. Paddon, and A. G. Hinnebusch. 1993. Guanine nucleotide exchange factor for eIF-2 in yeast: genetic and biochemical analysis of interactions between essential subunits GCD2, GCD6, and GCD7 and regulatory subunit GCN3. Mol. Cell. Biol. 13:4618-4631.
5. Chong, K. L., L. Feng, K. Schappert, E. Meurs, T. F. Donahue, J. D. Friesen, A. G. Hovanessian, and B. R. G. Williams. 1992. Human p68 kinase exhibits growth suppression in yeast and homology to the translational regulator GCN2. EMBO J. 11:1553-1562.
6. Christianson, T. W., R. S. Sikorski, M. Dante, J. H. Shero, and P. Hieter. 1992. Multifunctional yeast high-copy-number shuttle vectors. Gene 110: 119-122.
7. Cigan, A. M., J. L. Bushman, T. R. Boal, and A. G. Hinnebusch. 1993. A protein complex of translational regulators of CCN4 is the guanine nucleotide exchange factor for eIF-2 in yeast. Proc. Natl. Acad. Sci. USA 90:5350-5354.
8. Cigan, A. M., M. Foiani, E. M. Hannig, and A. G. Hinnebusch. 1991. Complex formation by positive and negative translational regulators of GCN4. Mol. Cell. Biol. 11:3217-3228.
9. Dever, T. E., J. J. Chen, G. N. Barber, A. M. Cigan, L. Feng, T. F. Donahue, I. M. London, M. G. Katze, and A. G. Hinnebusch. 1993. Mammalian eukaryotic initiation factor 2α kinases functionally substitute for GCN2 in the GCN4 translational control mechanism of yeast. Proc. Natl. Acad. Sci. USA 90:4616-4620.
10. Dever, T. E., L. Feng, R. C. Wek, A. M. Cigan, T. D. Donahue, and A. G. Hinnebusch. 1992. Phosphorylation of initiation factor 2α by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast. Cell 68:585-596.
11. i ternary complexes. Mol. Cell. Biol. 15:6351-6363.
12. Garcia-Barrio, M. T., T. Naranda, R. Cuesta, A. G. Hinnebusch, J. W. B. Hershey, and M. Tamanimel. 1995. GCD10, a translational repressor of GCN4, is the RNA-binding subunit of eukaryotic translation initiation factor-3. Genes Dev. 9:1781-1796.
13. Green, N., H. Alexander, A. Olson, S. Alexander, T. M. Shinnick, J. G. Sutcliffe, and R. A. Lerner. 1982. Immunogenic structure of the influenza virus hemagglutinin. Cell 28:477-487.
14. Hannig, E. H., N. P. Williams, R. C. Wek, and A. G. Hinnebusch. 1990. The translational activator GCN3 functions downstream from GCN1 and GCN2 in the regulatory pathway that couples GCN4 expression to amino acid availability in Saccharomyces cerevisiae. Genetics 126:549-562.
15. Hannig, E. M., A. M. Cigan, B. A. Freeman, and T. G. Kinzy. 1992. GCD11, a negative regulator of GCN4 expression, encodes the gamma subunit of eIF-2 in Saccharomyces cerevisiae. Mol. Cell. Biol. 13:506-520.
16. Hill, D. E., and K. Struhl. 1988. Molecular characterization of GCD1, a yeast gene required for general control of amino acid biosynthesis and cell-cycle initiation. Nucleic Acids Res. 16:9253-9265.
17. Hinnebusch, A. G. 1992. General and pathway-specific regulatory mechanisms controlling the synthesis of amino acid biosynthetic enzymes in Saccharomyces cerevisiae, p. 319-414. In E. W. Jones, J. R. Broach, and T. R. Pringle (ed.), The molecular and cellular biology of the yeast Saccharomyces: gene expression. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
18. Hinnebusch, A. G. 1993. Gene-specific translational control of the yeast GCN4 gene by phosphorylation of eukaryotic initiation factor 2. Mol. Microbiol. 10:215-223.
19. Hinnebusch, A. G. 1994. The eIF-2α kinases: regulators of protein synthesis in starvation and stress. Cell Biol. 5:417-426.
20. Hinnebusch, A. G. 1994. Translational control of GCN4: an in vivo barometer of initiation factor activity. Trends Biochem. Sci. 19:409-414.
21. Hinnebusch, A. G. 1996. Translational control of GCN4: gene-specific regulation by phosphorylation of eIF2, p. 199-244. In J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
22. Ito, H., Y. Fukada, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bactcriol. 153:163-168.
23. Jones, E. W. 1991. Tackling the protease problem in Saccharomyces cerevisiae. Methods Enzymol. 194:428-453.
24. Koerner, T. J., J. E. Hill, A. M. Myers, and A. Tzagoloff. 1991. High-expression vectors with multiple cloning sites for construction of trpE fusion genes: pATH vectors. Methods Enzymol. 194:477-490.
25. London, I. M., D. H. Levin, R. L. Matts, N. S. B. Thomas, R. Petryshyn, and J. J. Chen. 1987. Regulation of protein synthesis, p. 359-380. In P. D. Boyer and E. G. Krebs (ed.), The enzymes, vol. 18. Academic Press, New York.
26. Paddon, C. J., E. M. Hannig, and A. G. Hinnebusch. 1989. Amino acid sequence similarity between GCN3 and GCD2, positive and negative translational regulators of GCN4: evidence for antagonism by competition. Genetics 122:551-559.
27. Pavitt, G. D., W. Yang, and A. G. Hinnebusch. Identification of amino acids in homologous segments of 3 subunits of the guanine nucleotide exchange factor eIF2B required for translational regulation by phosphorylation of eukaryotic translation initiation factor 2. Submitted for publication.
28. Ramirez, M., R. C. Wek, C. R. Vazquez de Aldana, B. M. Jackson, B. Freeman, and A. G. Hinnebusch. 1992. Mutations activating the yeast eIF-2α kinase GCN2: isolation of alleles altering the domain related to histidyl-tRNA synthetases. Mol. Cell. Biol. 12:5801-5815.
29. 28a. Romano, P., and A. G. Hinnebusch, Unpublished data.
30. Rose, M. D., F. Winston, and P. Hieter. 1990. Methods in yeast genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
31. Rowlands, A. G., R. Panniers, and E. C. Henshaw. 1988. The catalytic mechanism of guanine nucleotide exchange factor action and competitive inhibition by phosphorylated eukaryotic initiation factor 2. J. Biol. Chem. 263:5526-5533.
32. Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463-5467.
33. Sherman, F., G. R. Fink, and C. W. Lawrence. 1974. Methods of yeast genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
34. Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19-27.
35. Taylor, S. S. 1989. cAMP-dependent protein kinase. Model for an enzyme family. J. Biol. Chem. 264:8443-8446.
36. Vazquez de Aldana, C. R., and A. G. Hinnebusch. 1994. Mutations in the GCD7 subunit of yeast guanine nucleotide exchange faclor eIF-2B overcome the inhibitory effects of phosphorylated eIF-2 on translation initiation. Mol. Cell. Biol. 14:3208-3222.