Characterization of the Saccharomyces cerevisiae YMR318C (ADH6) gene product as a broad specificity NADPH-dependent alcohol dehydrogenase: relevance in aldehyde reduction

ABSTRACT 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 ADH2-6c 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/adr6-1strains 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 ADH2-6c 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.

Download Full-text

Overexpression of the CDC25 gene, an upstream element of the ras/adenylyl cyclase pathway in Saccharomyces cerevisiae, allows immunological identification and characterization of its gene product

Biochemical and Biophysical Research Communications ◽

10.1016/s0006-291x(05)80173-1 ◽

1990 ◽

Vol 172 (1) ◽

pp. 61-69 ◽

Cited By ~ 14

Author(s):

Marco Vanoni ◽

Monica Vavassori ◽

Gianni Frascotti ◽

Enzo Martegani ◽

Lilia Alberghina

Keyword(s):

Saccharomyces Cerevisiae ◽

Adenylyl Cyclase ◽

Gene Product ◽

Its Gene ◽

Upstream Element ◽

Identification And Characterization ◽

Immunological Identification

Download Full-text

Characterization of the Kluyveromyces marxianus strain DMB1 YGL157w gene product as a broad specificity NADPH-dependent aldehyde reductase

AMB Express ◽

10.1186/s13568-015-0104-9 ◽

2015 ◽

Vol 5 (1) ◽

Cited By ~ 2

Author(s):

Hironaga Akita ◽

Masahiro Watanabe ◽

Toshihiro Suzuki ◽

Nobutaka Nakashima ◽

Tamotsu Hoshino

Keyword(s):

Gene Product ◽

Kluyveromyces Marxianus ◽

Aldehyde Reductase ◽

Broad Specificity

Download Full-text

The INO2 and INO4 loci of Saccharomyces cerevisiae are pleiotropic regulatory genes.

Molecular and Cellular Biology ◽

10.1128/mcb.4.11.2479 ◽

1984 ◽

Vol 4 (11) ◽

pp. 2479-2485 ◽

Cited By ~ 53

Author(s):

B S Loewy ◽

S A Henry

Keyword(s):

Saccharomyces Cerevisiae ◽

Gene Product ◽

Regulatory Genes ◽

Wild Type ◽

Inositol 1 ◽

Cytoplasmic Enzyme ◽

Pleiotropic Phenotype ◽

Reduced Rate ◽

Phosphate Synthase

We isolated a mutant of Saccharomyces cerevisiae defective in the formation of phosphatidylcholine via methylation of phosphatidylethanolamine. The mutant synthesized phosphatidylcholine at a reduced rate and accumulated increased amounts of methylated phospholipid intermediates. It was also found to be auxotrophic for inositol and allelic to an existing series of ino4 mutants. The ino2 and ino4 mutants, originally isolated on the basis of an inositol requirement, are unable to derepress the cytoplasmic enzyme inositol-1-phosphate synthase (myo-inositol-1-phosphate synthase; EC 5.5.1.4). The INO4 and INO2 genes were, thus, previously identified as regulatory genes whose wild-type product is required for expression of the INO1 gene product inositol-1-phosphate synthase (T. Donahue and S. Henry, J. Biol. Chem. 256:7077-7085, 1981). In addition to the identification of a new ino4-allele, further characterization of the existing series of ino4 and ino2 mutants, reported here, demonstrated that they all have a reduced capacity to convert phosphatidylethanolamine to phosphatidylcholine. The pleiotropic phenotype of the ino2 and ino4 mutants described in this paper suggests that the INO2 and INO4 loci are involved in the regulation of phospholipid methylation in the membrane as well as inositol biosynthesis in the cytoplasm.

Download Full-text