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Gene Expression

Dimerization by Translation Initiation Factor 2 Kinase GCN2 Is Mediated by Interactions in the C-Terminal Ribosome-Binding Region and the Protein Kinase Domain

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Pages 2697-2711 | Received 21 Nov 1997, Accepted 02 Feb 1998, Published online: 28 Mar 2023

REFERENCES

  • Bardwell, L., A. J. Cooper, and E. C. Friedberg 1992. Stable and specific association between the yeast recombination and DNA repair proteins RAD1 and RAD10 in vitro. Mol. Cell. Biol. 12: 3041–3049.
  • Boeke, J. D., F. LaCroute, and G. R. Fink 1984. A positive selection for mutants lacking orotidine-5′-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance. Mol. Gen. Genet. 197: 345–346.
  • 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.
  • Cesareni, G., and J. A. H. Murray Plasmid vectors carrying the replication origin of filamentous single-stranded phages Genetic engineering: principles and methods In: Setlow, J. K., and A. Hollaender91987135–154Plenum Press, New York, N.Y.
  • Cusack, S., M. Hartlein, and R. Leberman 1991. Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases. Nucleic Acids Res. 19: 3489–3498.
  • Dever, T. Personal communication.
  • 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.
  • Diallinas, G., and G. Thireos 1994. Genetic and biochemical evidence for yeast GCN2 protein kinase polymerization. Gene 143: 21–27.
  • Driscoll-Penn, M., G. Thireos, and H. Greer 1984. Temporal analysis of general control of amino acid biosynthesis in Saccharomyces cerevisiae: role of positive regulatory genes in initiation and maintenance of mRNA derepression. Mol. Cell. Biol. 4: 520–528.
  • Garcia-Barrio, M. T., and A. G. Hinnebusch. Unpublished observations.
  • Gietz, R. D., A. R. Willems, and R. A. Woods 1995. Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure. Yeast 11: 355–360.
  • Golemis, E. A., J. Gyuris, and R. Brent 1996. Interaction trap/two-hybrid system to identify interacting proteins Current protocols in molecular biology. In: Ausubel, F. M., R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl20.1.1–20.1.28John Wiley & Sons, Inc., New York, N.Y.
  • Gyuris, J., E. Golemis, H. Chertkov, and R. Brent 1993. Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2. Cell 75: 791–803.
  • Hanks, S. K., and T. Hunter 1995. The eukaryotic protein kinase superfamily The protein kinase facts book. In: Hardie, G., and S. Hanks7–47Academic Press, Inc., San Diego, Calif.
  • Heldin, C.-H. 1995. Dimerization of cell surface receptors in signal transduction. Cell 80: 213–223.
  • Hershey, J. W. B. 1991. Translational control in mammalian cells. Annu. Rev. Biochem. 60: 717–755.
  • Hinnebusch, A. G. 1994. The eIF-2α kinases: regulators of protein synthesis in starvation and stress. Cell Biol. 5: 417–426.
  • Hinnebusch, A. G. 1996. Translational control of GCN4: gene-specific regulation by phosphorylation of eIF2 Translational control. In: Hershey, J. W. B., M. B. Mathews, and N. Sonenberg199–244Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
  • Kozak, M. 1983. Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles. Microbiol. Rev. 47: 1–45.
  • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685.
  • Lanker, S., J. L. Bushman, A. G. Hinnebusch, H. Trachsel, and P. P. Mueller 1992. Autoregulation of the yeast lysyl-tRNA synthetase gene GCD5/KRS1 by translational and transcriptional control mechanisms. Cell 70: 647–657.
  • Lucchini, G., A. G. Hinnebusch, C. Chen, and G. R. Fink 1984. Positive regulatory interactions of the HIS4 gene of Saccharomyces cerevisiae. Mol. Cell. Biol. 4: 1326–1333.
  • Marton, M. J., C. R. Vazquez de Aldana, H. Qiu, K. Chakraburtty, and A. G. Hinnebusch 1997. Evidence that GCN1 and GCN20, translational regulators of GCN4, function on elongating ribosomes in activation of the eIF2α kinase GCN2. Mol. Cell. Biol. 17: 4474–4489.
  • Mathews, M. B. 1993. Viral evasion of cellular defense mechanisms: regulation of the protein kinase DAI by RNA effectors. Semin. Virol. 4: 247–257.
  • Merrick, W. C., and J. W. B. Hershey 1996. The pathway and mechanism of eukaryotic protein synthesis Translational control. In: Hershey, J. W. B., M. B. Mathews, and N. Sonenberg31–69Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
  • Messenguy, F., and J. Delforge 1976. Role of transfer ribonucleic acids in the regulation of several biosynthesis in Saccharomyces cerevisiae. Eur. J. Biochem. 67: 335–339.
  • Pharmacia. 1996. GST Gene Fusion System Manual. Pharmacia, Uppsala, Sweden.
  • Qiu, H., and A. G. Hinnebusch. Unpublished observations.
  • Ramirez, M., R. C. Wek, and A. G. Hinnebusch 1991. Ribosome association of GCN2 protein kinase, a translational activator of the GCN4 gene of Saccharomyces cerevisiae. Mol. Cell. Biol. 11: 3027–3036.
  • 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.
  • Romano, P. R., M. T. Garcia-Barrio, X. Zhang, Q. Wang, D. R. Taylor, F. Zhang, C. Herring, M. B. Mathews, J. Qin, and A. G. Hinnebusch 1998. Autophosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2α kinases PKR and GCN2. Mol. Cell. Biol. 18: 2282–2297.
  • Schnarr, M., M. Granger-Schnarr, S. Hurstel, and J. Pouyet 1988. The carboxy terminal domain of the LexA repressor oligomerises essentially as the entire protein. FEBS Lett. 234: 56–60.
  • Sherman, F., G. R. Fink, and C. W. Lawrence 1974. Methods of yeast genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
  • Towbin, H., T. Staehelin, and J. Gordon 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76: 4350–4354.
  • Vazquez de Aldana, C. R., R. C. Wek, P. San Segundo, A. G. Truesdell, and A. G. Hinnebusch 1994. Multicopy tRNA genes functionally suppress mutations in yeast eIF-2α kinase GCN2: evidence for separate pathways coupling GCN4 expression to uncharged tRNA. Mol. Cell. Biol. 14: 7920–7932.
  • Wek, R. C., B. M. Jackson, and A. G. Hinnebusch 1989. Juxtaposition of domains homologous to protein kinases and histidyl-tRNA synthetases in GCN2 protein suggests a mechanism for coupling GCN4 expression to amino acid availability. Proc. Natl. Acad. Sci. USA 86: 4579–4583.
  • Wek, R. C., M. Ramirez, B. M. Jackson, and A. G. Hinnebusch 1990. Identification of positive-acting domains in GCN2 protein kinase required for translational activation of GCN4 expression. Mol. Cell. Biol. 10: 2820–2831.
  • Wek, S. A., S. Zhu, and R. C. Wek 1995. The histidyl-tRNA synthetase-related sequence in the eIF-2α protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids. Mol. Cell. Biol. 15: 4497–4506.
  • Zhang, F., M. Kirouac, N. Zhu, A. G. Hinnebusch, and R. J. Rolfes 1997. Evidence that complex formation by Bas1p and Bas2p (Pho2p) unmasks the activation function of Bas1p in an adenine-repressible step of ADE gene transcription. Mol. Cell. Biol. 17: 3272–3283.
  • Zhu, S., A. Y. Sobolev, and R. C. Wek 1996. Histidyl-tRNA synthetase-related sequences in GCN2 protein kinase regulate in vitro phosphorylation of eIF-2. J. Biol. Chem. 271: 24989–24994.

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