Letter | Published:

Phenotypic suppression and misreading in Saccharomyces cerevisiae

Naturevolume 277pages146148 (1979) | Download Citation



A NUMBER of antibiotics and other inhibitors have been useful in genetic and biochemical analyses of the protein-synthesising machinery of prokaryotic and eukaryotic organisms. Aminoglycoside antibiotics have been shown to be particularly helpful in this respect, especially in identifying ribosomal protein cistrons in bacteria. The aminoglycosides cause extensive misreading of the RNA code words in vitro1 and suppress many nonsense and missense mutations in E. coli2 phenotypically. The misreading observed in cell-free translation is believed to be the basis for the phenotypic suppression, although the exact mechanism is not known. Apart from a report of suppression of a single mutation in yeast by streptomycin3, there have been no demonstrations of phenotypic suppression in eukaryotic organisms. Earlier studies of mistranslation in vitro in eukaryotic systems indicated that this phenomenon is rare. Streptomycin did not cause misreading with cytoplasmic ribosomes of rat liver4, rabbit spleen5, chicken liver6 or yeast7; neomycin had no effect in rabbit reticulocyte extracts4 and only a slight effect in the yeast and chicken liver systems6,7. These results suggested that translation in higher organisms functions with higher fidelity than that in bacteria. Nevertheless, aminoglycoside antibiotics have recently been shown to cause extensive translational misreading in vitro in systems derived from Tetrahymena8, wheat embryo9, and cultured human cells10.

Access optionsAccess options

Rent or Buy article

Get time limited or full article access on ReadCube.


All prices are NET prices.


  1. 1

    Davies, J., Gorini, L. & Davis, B. D. Molec. Pharmac. 1, 93–106 (1965).

  2. 2

    Gorini, L. In Ribosomes (eds Nomura, M., Tissieres, T. & Lengyel, P.). 791–803 (Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, 1974).

  3. 3

    Bayliss, F. T. & Vinopal, R. T. Nature 174, 1339–1341 (1971).

  4. 4

    Weinstein, I. B., Ochoa, M. Jr & Friedman, S. M. Biochemistry 5, 3332–3339 (1966).

  5. 5

    Stavy, L. Proc. natn. Acad. Sci. U.S.A. 61, 347–353 (1968).

  6. 6

    Kurtz, D. I. Biochemistry 13, 572–577 (1974).

  7. 7

    Schlanger, G. & Friedman, S. M. J. Bact. 115, 129–138 (1973).

  8. 8

    Palmer, E. & Wilhelm, J. M. Cell 13, 329–324 (1978).

  9. 9

    Wilhelm, J. M., Pettit, S. E. & Jessop, J. J. Biochemistry 17, 1143–1149 (1978).

  10. 10

    Wilhelm, J. M., Jessop, J. J. & Pettit, S. E. Biochemistry 17, 1149–1153 (1978).

  11. 11

    Singh, A. & Sherman, F. Genetics 81, 75–97 (1975).

  12. 12

    Gorini, L. & Davies, J. Curr. Top. Microbiol. Immun. 44, 100–122 (1968).

  13. 13

    Cox, B. S. Heredity 26, 211–232 (1971).

  14. 14

    Liebman, S. W., Stewart, J. W. & Sherman, F. J. molec. Biol. 94, 595–610.

  15. 15

    Culbertson, M. R., Charnas, L., Johnson, M. T. & Fink, G. R. Genetics 86, 745–764.

  16. 16

    Schindler, D. thesis, Univ. Wisconsin, Madison (1976).

  17. 17

    Grant, P. G., Sanchez, L. & Jimenez, A. J. Bact. 120, 1308–1314 (1974).

  18. 18

    Gonzalez, A., Jimenez, A., Vazquez, D., Davies, J. E. & Schindler, D. Biochim. biophys. Acta (in the press).

Download references

Author information


  1. Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin-Madison, Madison, Wisconsin, 53706



  1. Search for ARJUN SINGH in:

  2. Search for DORIS URSIC in:

  3. Search for JULIAN DAVIES in:

About this article

Publication history



Issue Date



Further reading


By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.