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Gene Expression

A Segment of mRNA Encoding the Leader Peptide of the CPA1 Gene Confers Repression by Arginine on a Heterologous Yeast Gene Transcript

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Pages 2378-2390 | Received 26 Jul 1993, Accepted 04 Jan 1994, Published online: 30 Mar 2023

REFERENCES

  • Abastado, J. P., P. F. Miller, B. M. Jackson, and A. G. Hinnebusch. 1991. Suppression of ribosomal reinitiation at upstream open reading frames in amino acid-starved cells forms the basis for GCN4 translational control. Mol. Cell. Biol. 11:486–496.
  • Beacham, I. R., B. W. Schweitzer, H. M. Warrick, and J. Carbon. 1984. The nucleotide sequence of the yeast ARG4 gene. J. Mol. Biol. 29:271–279.
  • Birnboim, H. C. 1983. A rapid alkaline extraction method for the isolation of plasmid DNA. Methods Enzymol. 100:243–255.
  • Bonneaud, N., O. Ozier-Kalogeropoulos, G. Li, M. Labouesse, L. Minvielle-Sebastia, and F. Lacroute. 1991. A family of low and high copy replicative, integrative and single stranded S. cerevi-siae/E. coli shuttle vectors. Yeast 7:609–615.
  • Casadaban, M. J., J. Chou, and S. N. Cohen. 1980. In vitro gene fusions that join an enzymatically active β-galactosidase segment to amino-terminal fragments of exogenous proteins: Escherichia coli plasmid vectors for the detection and cloning of translational initiation signals. J. Bacteriol. 143:971–980.
  • Cigan, A. M., E. K. Pabich, L. Feng, and T. F. Donahue. 1989. Yeast translation initiation suppressor sui2 encodes the a subunit of eukaryotic initiation factor 2 and shares identity with the human a subunit. Proc. Natl. Acad. Sci. USA 86:2784–2788.
  • Crabeel, M., R. Lavalle, and N. Glansdorff. 1990. Arginine specific repression in Saccharomyces cerevisiae: kinetic data on ARG1 and ARG3 mRNA transcription and stability support a transcriptional control mechanism. Mol. Cell. Biol. 10:1226–1233.
  • Delbecq, P., M. Werner, A. Feller, and A. Piérard. 1990. Translational control by arginine of yeast gene CPA1. Yeast 6:S395.
  • Delbecq, P., F. Messenguy, M. Werner, A. Feller, and A. Piérard. 1992. Translational control of yeast gene CPA1: analysis of its leader sequence and effect of mutations in initiation factor eIF-2 on its expression. Yeast 8:S60.
  • Delforge, J., F. Messenguy, and J.-M. Wiame. 1975. The regulation of arginine biosynthesis in Saccharomyces cerevisiae: the specificity of argR mutations and the general control of amino acid biosynthesis. Eur. J. Biochem. 57:231–239.
  • Dever, T. E., L. Feng, R. C. Wek, A. M. Cigan, T. F. Donahue, and A. G. Hinnebusch. 1992. Phosphorylation of initiation factor 2a by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast. Cell 68:585–596.
  • Hinnebusch, A. G. 1984. Evidence for translational regulation of the activator of general amino acid control in yeast. Proc. Natl. Acad. Sci. USA 81:6442–6446.
  • Hinnebusch, A. G. 1988. Mechanisms of gene regulation in the general control of amino acid biosynthesis in Saccharomyces cerevisiae. Microbiol. Rev. 52:248–273.
  • Hinnebusch, A. G. 1990. Involvement of an initiator factor and protein phosphorylation in translational control of GCN4 mRNA. TIBS Trends Biochem. Sci. 15:148–152.
  • Hinnebusch, A. G., and G. R. Fink. 1983. Positive regulation in the general amino acid control of S. cerevisiae. Proc. Natl. Acad. Sci. USA 80:5374–5378.
  • Kozak, M. 1989. The scanning model for translation: an update. J. Cell Biol. 108:229–241.
  • Lacroute, F., A. Piérard, M. Grenson, and J.-M. Wiame. 1965. The biosynthesis of carbamoylphosphate in Saccharomyces cerevisiae. J. Gen. Microbiol. 40:127–142.
  • Loppes, R., and C. Denis. 1983. Chloroplast and nuclear DNA fragments from Chlamydomonas promoting high frequency transformation of yeast. Curr. Genet. 7:473–480.
  • Maniatis, T., E. F. Fritsch, and J. Sambrook. 1982. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
  • Messenguy, F. 1979. Concerted repression of the synthesis of the arginine biosynthetic pathway by amino acids: a comparison between the regulatory mechanism controlling amino acid biosynthesis in bacteria and yeast. Mol. Gen. Genet. 169:85–95.
  • Messenguy, F., and E. Dubois. 1983. Participation of transcriptional and post-transcriptional regulatory mechanisms in the control of arginine metabolism in yeast. Mol. Gen. Genet. 189:148–156.
  • Messenguy, F., A. Feller, M. Crabeel, and A. Piérard. 1983. Control mechanisms acting at the transcriptional and post-transcriptional levels are involved in the synthesis of the arginine pathway carbamoylphosphate synthase of yeast. EMBO J. 2:1249–1254.
  • Messing, J. 1983. The new M13 vectors for cloning. Methods Enzymol. 101:20–78.
  • Micklus, M. J., and I. M. Stein. 1973. The colorimetric determination of mono and disubstituted guanidines. Anal. Biochem. 54:545–553.
  • Miller, P. F., and A. G. Hinnebusch. 1989. Sequences that surround the stop codons of upstream open reading frames in GCN4 mRNA determine their distinct functions in translational control. Genes Dev. 3:1217–1225.
  • Mueller, P. P., and A. G. Hinnebusch. 1986. Multiple upstream AUG codons mediate translational control of GCN4. Cell 45:201–207.
  • Nakamaye, K. L., and F. Eckstein. 1986. Inhibition of restriction endonuclease Ncil cleavage by phosphorothioate groups and its application to oligonucleotide-directed mutagenesis. Nucleic Acids Res. 14:9679–9698.
  • Piérard, A., F. Messenguy, A. Feller, and F. Hilger. 1979. Dual regulation of the synthesis of the arginine pathway carbamoylphosphate synthase of Saccharomyces cerevisiae by specific and general controls of amino acid biosynthesis. Mol. Gen. Genet. 174:163–171.
  • Piérard, A., and B. Schroter. 1978. Structure-function relationships in the arginine pathway carbamoylphosphate synthase of Saccharomyces cerevisiae. J. Bacteriol. 134:167–176.
  • Ramos, F., and J.-M. Wiame. 1979. Synthesis and activation of asparaginase in asparagine auxotrophs of Saccharomyces cerevisiae. Eur. J. Biochem. 94:409–417.
  • Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463–5467.
  • Sherman, F., G. R. Fink, and J. B. Hicks. 1986. Methods in yeast genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
  • Taylor, J. W., and F. Eckstein. 1985. The rapid generation of oligonunucleotide-directed mutations at high frequency using phophorothioate-modified DNA. Nucleic Acids Res. 13:8765–8785.
  • Thireos, G., M. Driscoll-Penn, and H. Greer. 1984. 5′ untranslated sequences are required for translational control of a yeast regulatory gene. Proc. Natl. Acad. Sci. USA 81:5096–5100.
  • Thuriaux, P., F. Ramos, A. Piérard, M. Grenson, and J.-M. Wiame. 1972. Regulation of the carbamoylphosphate synthetase belonging to the arginine biosynthetic pathway of Saccharomyces cerevisiae. J. Mol. Biol. 67:277–287.
  • Werner, M., A. Feller, P. Delbecq, and A. Piérard. 1990. Translational control by arginine of yeast gene CPA1. NATO ASI Ser. Ser. H 49:337–346.
  • Werner, M., A. Feller, F. Messenguy, and A. Piérard. 1987. The leader peptide of yeast gene CPA1 is essential for the translational repression of its expression. Cell 49:805–813.
  • Werner, M., A. Feller, and A. Piérard. 1985. Nucleotide sequence of yeast gene CPA1 encoding the small subunit of arginine-pathway carbamoyl-phosphate synthetase: homology of the deduced amino acid sequence to other glutamine amidotransferases. Eur. J. Biochem. 146:371–381.

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