Identification of Positive-Acting Domains in GCN2 Protein Kinase Required for Translational Activation of GCN4 Expression

Literature Cited

• Bischoff, J. R., and C. E. Samuel. 1985. Mechanism of interferon action: the interferon-induced phosphoprotein P1 possesses a double-stranded RNA-dependent ATP-binding site. J. Biol. Chem. 260:8237–8239.
   PubMedGoogle Scholar
• Booher, R., and D. Beach. 1986. Site-specific mutagenesis of cdc2+, a cell cycle control gene of the fission yeast Schizosac-charomyces pombe. Mol. Cell. Biol. 6:3523–3530.
   PubMedGoogle Scholar
• Booher, R. N., C. E. Alfa, J. S. Hyams, and D. H. Beach. 1989. The fission yeast cdc2/cdc13/suc1 protein kinase: regulation of catalytic activity and nuclear localization. Cell 58:485–497.
   PubMed Web of Science ®Google Scholar
• Botstein, D., S. C. Falco, S. E. Stewart, M. Brennan, S. Scherer, D. T. Stinchcomb, K. Struhl, and R. W. Davis. 1979. Sterile host yeasts (SHY): a eukaryotic system of biological containment for recombinant DNA experiments. Gene 8:17–24.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Brenner, S. 1987. Phosphotransferase sequence homology. Nature (London) 329:21.
   PubMedGoogle Scholar
• Broach, J., J. Strathern, and J. Hicks. 1979. Transformation in yeast: development of a hybrid cloning vector, and isolation of the CAN1 gene. Gene 8:121–133.
   PubMed Web of Science ®Google Scholar
• Donahue, T. F., P. J. Farabaugh, and G. R. Fink. 1982. The nucleotide sequence of the HIS4 region of yeast. Gene 18:47–59.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMedGoogle Scholar
• Edelman, A. M., D. K. Blumenthal, and E. G. Krebs. 1987. Protein serine/threonine kinases. Annu. Rev. Biochem. 56:567–613.
   PubMed Web of Science ®Google Scholar
• Feinberg, A. P., and B. Vogelstein. 1984. Addendum: a technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 137:266–267.
   PubMed Web of Science ®Google Scholar
• Gould, K. L., and P. Nurse. 1989. Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase regulates entry into mitosis. Nature (London) 342:39–45.
   PubMed Web of Science ®Google Scholar
• Hanks, S. K., A. M. Quinn, and T. Hunter. 1988. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 241:41–52.
   Google Scholar
• Hannig, E. M., and A. G. Hinnebusch. 1988. Molecular analysis of GCN3, a translational activator of GCN4: evidence for posttranslational control of GCN3 regulatory function. Mol. Cell. Biol. 8:4808–4820.
   PubMedGoogle Scholar
• Harlow, E., and D. Lane. 1988. Antibodies: a laboratory man ual. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Hayman, M. J., G. Kitchener, J. Knight, J. McMahon, R. Watson, and H. Beug. 1986. Analysis of the autophosphorylation activity of transformation-defective mutants of avian erythroblastosis virus. Virology 150:270–275.
   PubMedGoogle Scholar
• Hinnebusch, A. G. 1985. A hierarchy of trans-acting factors modulate translation of an activator of amino acid biosynthetic genes in yeast. Mol. Cell. Biol. 5:2349–2360.
   PubMed Web of Science ®Google Scholar
• Hinnebusch, A. G. 1986. The general control of amino acid biosynthetic genes in the yeast Saccharomyces cerevisiae. Crit. Rev. Biochem. 21:277–317.
   PubMed Web of Science ®Google Scholar
• Hinnebusch, A. G. 1988. Mechanisms of gene regulation in the general control of amino acid biosynthesis in Saccharomyces cerevisiae. Microbiol. Rev. 52:248–273.
   PubMedGoogle Scholar
• Hinnebusch, A. G., and G. R. Fink. 1983. Positive regulation in the general amino acid control of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 80:5374–5378.
   PubMed Web of Science ®Google Scholar
• Hinnebusch, A. G., and G. R. Fink. 1983. Repeated DNA sequences upstream from HIS1 also occur at several other co-regulated genes in Saccharomyces cerevisiae. J. Biol. Chem. 258:5238–5247.
   PubMed Web of Science ®Google Scholar
• Hoffman, C. S., and F. Winston. 1987. A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli. Gene 57:267–272.
   PubMed Web of Science ®Google Scholar
• Hunter, T. 1987. A tail of two src's: mutatis mutandis. Cell 49:1–4.
   PubMed Web of Science ®Google Scholar
• Ito, H., Y. Fukada, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163–168.
   PubMed Web of Science ®Google Scholar
• Kikkawa, U., A. Kishimoto, and Y. Nishizuka. 1989. The protein kinase C family: heterogeneity and its implications. Annu. Rev. Biochem. 58:31–44.
   PubMed Web of Science ®Google Scholar
• Klionsky, D. J., L. M. Banta, and S. D. Emr. 1988. Intracellular sorting and processing of a yeast vacuolar hydrolase: proteinase A propeptide contains vacuolar targeting information. Mol. Cell. Biol. 8:2105–2116.
   PubMedGoogle Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Maniatis, T., E. F. Fritsch, and J. Sambrook. 1982. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Niederberger, P., M. Aebi, and R. Huetter. 1986. Identification and characterization of four new GCD genes in Saccharomyces cerevisiae. Curr. Genet. 10:657–664.
   PubMedGoogle Scholar
• Rapp, U. R., G. Heidecker, M. Huleihel, J. L. Cleveland, W. C. Choi, T. Pawson, J. N. Ihle, and W. B. Anderson. 1988. raf family serine/ threonine protein kinases in mitogen signal transduction. Cold Spring Harbor Symp. Quant. Biol. 53:173–184.
   PubMedGoogle Scholar
• Reed, S. I., J. A. Hadwiger, and A. T. Lorincz. 1985. Protein kinase activity associated with the product of the yeast cell division cycle gene CDC28. Proc. Natl. Acad. Sci. USA 82:4055–4059.
   PubMed Web of Science ®Google Scholar
• Rose, M. D., and G. R. Fink. 1987. KAR1, a gene required for function of both intranuclear and extranuclear microtubules in yeast. Cell 48:1047–1060.
   PubMed Web of Science ®Google Scholar
• Rothstein, R. J. 1983. One-step gene disruption in yeast. Methods Enzymol. 101:202–211.
   PubMed Web of Science ®Google Scholar
• Roussel, M. F., T. J. Dull, C. W. Rettenmeir, P. Ralph, A. Ullrich, and C. J. Sherr. 1987. Transforming potential of the c-fms-oncogene (CSF-1 receptor). Nature (London) 325:549–552.
   PubMed Web of Science ®Google Scholar
• Roussou, I., G. Thireos, and B. M. Hauge. 1988. Transcriptional- translational regulatory circuit in Saccharomyces cerevisiae which involves the GCN4 transcriptional activator and the GCN2 protein kinase. Mol. Cell. Biol. 8:2132–2139.
   PubMedGoogle Scholar
• Schimmel, P. R., and D. Soll. 1979. Aminoacyl-tRNA synthetases: general features and recognition of transfer RNAs. Annu. Rev. Biochem. 48:601–648.
   PubMed Web of Science ®Google Scholar
• Sherman, F., G. R. Fink, and C. W. Lawrence. 1974. Methods of yeast genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designated for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19–27.
   PubMed Web of Science ®Google Scholar
• Stanton, V. P., D. W. Nichols, A. P. Laudano, and G. M. Cooper. 1989. Definition of human raf amino-terminal regulatory region by deletion mutagenesis. Mol. Cell. Biol. 9:639–647.
   PubMed Web of Science ®Google Scholar
• Taylor, S. S. 1989. cAMP-dependent protein kinase. Model for an enzyme family. J. Biol. Chem. 264:8443–8446.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Williams, N. P., A. G. Hinnebusch, and T. F. Donahue. 1989. Mutations in the structural genes for eukaryotic initiation factors 2α and 2β of Saccharomyces cerevisiae disrupt transla tional control of GCN4 mRNA. Proc. Natl. Acad. Sci. USA 86:7515–7519.
   PubMed Web of Science ®Google Scholar
• Wittenberg, C., and S. I. Reed. 1988. Control of the yeast cell cycle is associated with assembly/disassembly of the Cdc28 protein kinase complex. Cell 54:1061–1072.
   PubMedGoogle Scholar
• Wolfner, M., D. Yep, F. Messenguy, and G. R. Fink. 1975. Integration of amino acid biosynthesis into the cell cycle of Saccharomyces cerevisiae. J. Mol. Biol. 96:273–290.
   PubMed Web of Science ®Google Scholar
• Yanisch-Perron, C., J. Vieira, and J. Messing. 1984. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103–119.
   Google Scholar
• Yarden, Y., and A. Ullrich. 1988. Growth factor receptor tyrosine kinases. Annu. Rev. Biochem. 57:443–478.
   PubMed Web of Science ®Google Scholar