The Molecular Consequences of Formaldehyde and Ethyl Methanesulfonate Mutagenesis in Drosophila: Analysis of Mutants in the Alcohol Dehydrogenase Gene

  • Allen R. Place
  • Cheeptip Benyajati
  • William Sofer
Part of the Experimental Biology and Medicine book series (EBAM, volume 3)


Chemical mutagenesis is a process whose analysis is complicated by the large number of possible reactions of mutagens and their byproducts with the genetic material, and the variety of pathways by which a mutational lesion can be repaired (1,2). One simplying factor, however, is that in some organisms the final result of a mutagenic pathway can be deduced, or directly assessed, by examination of the gene or gene product affected by the mutation. For example, by isolating and sequencing a protein that is a product of a mutant gene, one can deduce from the amino acid sequence, the nature of the nucleotide lesion. Similarly, by comparing the nucleotide sequence of a mutant gene with its wild-type counterpart, one can directly determine the nature of the nucleotide defect.


Alcohol Dehydrogenase Tryptic Peptide Termination Codon Ethyl Methane Sulfonate Mutagenic Pathway 
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.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Auerbach, C. (1976) “Mutation Research”, John Wiley & Sons, Inc., New York.Google Scholar
  2. 2.
    Singer, B. (1977) J. Toxicology and Environmental Health 2, 1279–1295.CrossRefGoogle Scholar
  3. 3.
    Sofer, W. and Hatkoff, M.A. (1972) Genetics 72, 545–549.PubMedGoogle Scholar
  4. 4.
    O’Donnell, J., Gerace, L., Leister, F., and Sofer, W. (1975) Genetics 79, 73–83.PubMedGoogle Scholar
  5. 5.
    Thatcher, D.R. (1980) Biochem. J. 187, 875–886.Google Scholar
  6. 6.
    Benyajati, C., Place, A.R., Powers, D.A., and Sofer, W. (1981) Proc. Natl. Acad. Sci. USA 78, 2717–2721.PubMedCrossRefGoogle Scholar
  7. 7.
    Slizynski, B.M. (1945) Proc. Roy. Soc. Edin. 62B, 114–119.Google Scholar
  8. 8.
    O’Donnell, J., Mandel, H.C., Krauss, M., and Sofer, W. (1977) Genetics 86, 553–566.PubMedGoogle Scholar
  9. 9.
    Fishbein, J.C., Place, A.R., Ropson, I.J., Powers, D.A., and Sofer, W. (1980) Anal. Biochem. 108, 193–201.PubMedCrossRefGoogle Scholar
  10. 10.
    Reddy, A.R., Pelliccia, J.G., and Sofer, W. (1980) Biochem. Genet. 18, 338–351.CrossRefGoogle Scholar
  11. 11.
    Gough, N.M. and Adams, J.M. (1978) Biochemistry 17, 5560–5566.PubMedCrossRefGoogle Scholar
  12. 12.
    Lewis, E. and Bacher, F. (1968) Dros. Inf. Serv. 43, 193.Google Scholar
  13. 13.
    Jenkins, J.B. (1967) Mutation Res. 4, 90–92.PubMedCrossRefGoogle Scholar
  14. 14.
    Drake, J.W. (1970) “The Molecular Basis of Mutation”, Holden-Day, San Francisco.Google Scholar
  15. 15.
    Bautz, E. and Freese, E. (1960) Proc. Natl. Acad. Sci. USA 46, 1585–1594.PubMedCrossRefGoogle Scholar
  16. 16.
    Osborn, M., Person, S., Phillips, S., and Funk, F. (1967) J. Mol. Biol. 26, 437–448.PubMedCrossRefGoogle Scholar
  17. 17.
    Malling, H. V. and de Serres, F.J. (1970) Mutation Res. 6, 181–193.Google Scholar
  18. 18.
    Shukla, P.T. and Aurbach, C. (1981) Mutation Res. 83, 81–89.PubMedCrossRefGoogle Scholar

Copyright information

© The HUMANA Press Inc. 1982

Authors and Affiliations

  • Allen R. Place
    • 1
  • Cheeptip Benyajati
    • 2
  • William Sofer
    • 3
  1. 1.Department of BiologyUniversity of PennsylvaniaPhiladelphiaUSA
  2. 2.Frederick Cancer Research CenterFrederickUSA
  3. 3.Waksman InstituteRutgers UniversityPiscatawayUSA

Personalised recommendations