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Nucleic Acids Research, 1980, Vol. 8, No. 23 5649-5667
© 1980

MOLECULAR BIOLOGY

Alcohol dehydrogenase in Drosophila: isolation and characterization of messenger RNA and cDNA clone

Cheeptip Benyajati*,#, Nancy Wang**, Arjula Reddy+, Eric Weinberg{dagger} and William Sofer**

Department of Biology, The Johns Hopkins University Baltimore, MD 21218, USA

#To whom correspondence should be addressed

Received September 3, 1980.

The mRNA for alcohol dehydrogenase (ADH) in D. melanogaster has been identified by translation in a cell-free system. The in vitro synthesized polypeptide, specifically precipitated by anti-ADH antibody, has identical subunit molecular weight (25,000 daltons) and tryptic peptide profile to the in vivo synthesized ADH. The poly A containing ADH-mRNA has been purified by specific precipitation of ADH-polysomes using anti-ADH antibody and S. aureus. Transformation of E. coli with the dA-tailed ADH-mRNA-complementary DNA hybrid annealed to the dT-tailed pBR322 yielded one plasmid which has been identified as the ADH-cDNA clone. The identification involved hybridization selection of ADH-mRNA and in vitro translation, in situ hybridization to the Adh locus on salivary gland polytene chromosomes and DNA sequencing. This ADH-cDNA plasmid contains 349 bases of the C-terminal protein coding and 180 bases of the 3' untranslated region.

*Cancer Biology Program, Frederick Cancer Research Center, P.O. Box B, Frederick, MD 21701

**Waksman Institute of Microbiology, Rutgers University, P.O. Box 759, Piscataway, NJ 08854

+School of Life Sciences, Central University of Hyderabad, Hyderabad, India

{dagger}Department of Biology, Biology Bullding/G5, University of Pennsylvania, Philadelphia, PA 19104


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