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Translational Control of a Transcriptional Activator in the Regulation of Amino Acid Biosynthesis in Yeast

  • Alan G. Hinnebusch
  • Peter P. Mueller

Abstract

In the enteric bacteria, expression of many amino acid biosynthetic operons is adjusted to the availability of their amino acid end-products by a feedback regulatory mechanism that monitors the amount of the corresponding aminoacylated transfer RNAs (tRNAs) present in the cell. This feedback occurs by coupling transcription of each operon to efficient translation of a leader-encoded peptide rich in codons for the amino acid end-product. When the aminoacyl-tRNA concentration falls, ribosomes stall during translation of the leader peptide at codons for the limiting amino acid. This leads to a change in the messenger RNA (mRNA) secondary structure that suppresses a transcription termination signal, thus resulting in increased synthesis of full-length operon mRNA (reviewed in Kolter and Yanofsky1).

Keywords

Amino Acid Biosynthesis Starvation Condition Amino Acid Starvation Upstream Open Reading Frame General Amino Acid Control 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    Kolter, R., Yanofsky, C., 1982, Annu. Rev. Genet. 16: 113.PubMedCrossRefGoogle Scholar
  2. 2.
    Jones, E. W., Fink, G. R., 1983, in: The Molecular Biology of the Yeast Saccharomyces: Metabolism and Gene Expression (J. N. Strathern, E. W. Jones, J. R. Broach, eds.), pp. 181–300, Cold Spring Harbor Laboratory, Cold Spring Harbor, New York.Google Scholar
  3. 3.
    Hinnebusch, A. G., 1986, CRC Crit. Rev. Biochem 21: 277–317.PubMedCrossRefGoogle Scholar
  4. 4.
    Struhl, K., 1982, Nature (London) 300: 284.CrossRefGoogle Scholar
  5. 5.
    Donahue, T. F., Daves, R. S., Lucchini, G., Fink, G. R., 1983, Cell 32: 89.PubMedCrossRefGoogle Scholar
  6. 6.
    Lucchini, G., Hinnebusch, A. G., Chen, C., Fink, G. R., 1984, Mol. Cell. Biol. 4: 1326.PubMedGoogle Scholar
  7. 7.
    Hinnebusch, A. G., Lucchini, G., Fink, G. R., 1985, Proc. Natl. Acad. Sci. U.S.A. 82: 498.PubMedCrossRefGoogle Scholar
  8. 8.
    Driscoll Penn, M., Galgoci, B., Greer, H., 1983, Proc. Natl. Acad. Sci. U.S.A. 80: 2704.CrossRefGoogle Scholar
  9. 9.
    Wolfner, M., Yep, D., Messenguy, F., Fink, G. R., 1975, J. Mol. Biol. 96: 273.PubMedCrossRefGoogle Scholar
  10. 10.
    Hinnebusch, A. G., Fink, G. R., 1983, Proc. Natl. Acad. Sci. U.S.A. 80:5374.Google Scholar
  11. 11.
    Hinnebusch, A. G., 1984, Proc. Natl. Acad. Sci. U.S.A. 81: 6442.PubMedCrossRefGoogle Scholar
  12. 12.
    Hinnebusch. A. G., 1985, Mol. Cell. Biol. 5: 2349.PubMedGoogle Scholar
  13. 13.
    Hope, I. A., Struhl, K., 1985, Cell 43: 177.PubMedCrossRefGoogle Scholar
  14. 14.
    Thireos, G., Driscoll Penn, M., Greer, H., 1984, Proc. Natl. Acad. Sci. U.S.A. 81: 5096.PubMedCrossRefGoogle Scholar
  15. 15.
    Sherman, F., Stewart, J. W., 1983, in: The Molecular Biology of the Yeast Saccharomyces: Metabolism and Gene Expression (J.N. Strathern, E. W. Jones, J. R. Broach, eds.), pp. 301–334, Cold Spring Harbor Laboratory, Cold Spring Harbor, New York.Google Scholar
  16. 16.
    Zitomer, R. S., Walthall, D. A., Rymond, B. C., Hollenberg, C. P., 1984, Mol. Cell. Biol. 4: 1191.PubMedGoogle Scholar
  17. 17.
    Lomedico, P. T., McAndrew, S. J., 1982, Nature (London) 299: 221.CrossRefGoogle Scholar
  18. 18.
    Liu, C. C., Simonsen, C. C., Levinson, A. D., 1984, Nature (London) 309:82Google Scholar
  19. 19.
    Kozak, M., 1984, Nucleic Acids Res. 12: 3873.PubMedCrossRefGoogle Scholar
  20. 20.
    Johansen, H., Schumperli, D., Rosenberg, M., 1984, Proc. Natl. Acad. Sci. U.S.A. 81: 7698.CrossRefGoogle Scholar
  21. 21.
    Sherman, F., Stewart, J. W., 1975, in: Organization and Expression of the Eukaryotic Genome: Biochemical Mechanisms of Differentiation in Prokaryotes and Eukaryotes (Proceedings of the 10th FEBS Meeting) (G. Bernardi, F. Gros, eds.), p. 175, American Elsevier, New York.Google Scholar
  22. 22.
    Kozak, M., 1978, Cell 15: 1109.PubMedCrossRefGoogle Scholar
  23. 23.
    Mueller, P. P., Hinnebusch, A. G., 1986, Cell 45: 201–207.PubMedCrossRefGoogle Scholar
  24. 24.
    Nomura, M., Gourse, R., Baughman, G., 1984, Annu. Rev. Biochem. 53: 75.PubMedCrossRefGoogle Scholar
  25. 25.
    McKenzie, S. L., Henikoff, S., Meselson, M., 1975, Proc. Natl. Acad. Sci. U.S.A. 72: 1117.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Alan G. Hinnebusch
    • 1
  • Peter P. Mueller
    • 1
  1. 1.Laboratory of Molecular Genetics, National Institute of Child Health and Human DevelopmentNational Institutes of HealthBethesdaUSA

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