J. Jose Bonner* , Carol Parks, Janice Parker-Thornburg, Mark A. Mortin and Hugh R. B. Pelham, Department of Biology, Indiana University, Bloomington, Indiana, USA and Laboratory of Molecular Biology, Medical Research Council Centre, Cambridge
Alcohol Dehydrogenease (Adh) is an ideal enzyme for chemical selection of mutations affecting its expression, as Adh activity is required for survival of exposure to ethanol. Conversely, Adh activity renders exposure to 3-pentyne-l-ol lethal, thus allowing the selection of Adh-deficient flies. We have sought to adapt this system to the isolation of mutations affecting the expression of developmentally or metabolically regulated genes for which chemical selections do not already exist. We have used the heat shock system for our initial studies, as the heat shock genes are readily inducible in the laboratory, and the DNA sequences involved in their regulation are known. We have fused the 5’ flanking sequences of hsp70, and the nrst 200...
