The Identification and Characterization of ADR6, a Gene Required for Sporulation and for Expression of the Alcohol Dehydrogenase II Isozyme From Saccharomyces cerevisiae

Aileen K. W. Taguchi ¹ and Elton T. Young ¹

¹ Department of Biochemistry, University of Washington, Seattle, Washington 98195

The alcohol dehydrogenase II isozyme (enzyme, ADHII; structural gene, ADH2) of the yeast, Saccharomyces cerevisiae, is under stringent carbon catabolite control. This cytoplasmic isozyme exhibits negligible activity during growth in media containing fermentable carbon sources such as glucose and is maximal during growth on nonfermentable carbon sources. A recessive mutation, adr6-1, and possibly two other alleles at this locus, were selected for their ability to decrease Ty-activated ADH2-6 ^c expression. The adr6-1 mutation led to decreased ADHII activity in both ADH2-6^c and ADH2⁺ strains, and to decreased levels of ADH2 mRNA. Ty transcription and the expression of two other carbon catabolite regulated enzymes, isocitrate lyase and malate dehydrogenase, were unaffected by the adr6-1 mutation. adr6-1/adr6-1 strains were defective for sporulation, indicating that adr6 mutations may have pleiotropic effects. The sporulation defect was not a consequence of decreased ADH activity. Since the ADH2-6^c mutation is due to insertion of a 5.6-kb Ty element at the TATAA box, it appears that the ADR6⁺-dependent ADHII activity required ADH2 sequences 3' to or including the TATAA box. The ADH2 upstream activating sequence (UAS) was probably not required. The ADR6 locus was unlinked to the ADR1 gene which encodes another trans-acting element required for ADH2 expression.

This article has been cited by other articles:

				E. Di Mauro, S. G. Kendrew, and M. Caserta Two Distinct Nucleosome Alterations Characterize Chromatin Remodeling at the Saccharomyces cerevisiae ADH2 Promoter J. Biol. Chem., March 10, 2000; 275(11): 7612 - 7618. [Abstract] [Full Text] [PDF]

				S.-i. Numata, P. P. Claudio, C. Dean, A. Giordano, and C. M. Croce Bdp, a New Member of a Family of DNA-binding Proteins, Associates with the Retinoblastoma Gene Product Cancer Res., August 1, 1999; 59(15): 3741 - 3747. [Abstract] [Full Text] [PDF]

				Y.-C. Chiang, P. Komarnitsky, D. Chase, and C. L. Denis ADR1 Activation Domains Contact the Histone Acetyltransferase GCN5 and the Core Transcriptional Factor TFIIB J. Biol. Chem., December 13, 1996; 271(50): 32359 - 32365. [Abstract] [Full Text] [PDF]

				R F Herrscher, M H Kaplan, D L Lelsz, C Das, R Scheuermann, and P W Tucker The immunoglobulin heavy-chain matrix-associating regions are bound by Bright: a B cell-specific trans-activator that describes a new DNA-binding protein family. Genes & Dev., December 15, 1995; 9(24): 3067 - 3082. [Abstract] [PDF]

				S. Yoshinaga, C. Peterson, I Herskowitz, and K. Yamamoto Roles of SWI1, SWI2, and SWI3 proteins for transcriptional enhancement by steroid receptors Science, December 4, 1992; 258(5088): 1598 - 1604. [Abstract] [PDF]