The Control of Alcohol Dehydrogenase Isozyme Synthesis in Saccharomyces cerevisiae

1972 ◽  
Vol 50 (1) ◽  
pp. 35-43 ◽  
Author(s):  
P. Wendy Fowler ◽  
Alan J. S. Ball ◽  
David E. Griffiths
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Alcohol Dehydrogenase ◽  
Catabolite Repression ◽  
Isozyme Pattern ◽  
Isolated Mitochondria ◽  
Mechanical Disruption ◽  
Dehydrogenase Isozyme

Isozymes of alcohol dehydrogenase (ADH) from yeast were separated by discontinuous electrophoresis. Three major bands were observed: ADH-I, ADH-II, and a new band designated mito-ADH. Work with isolated mitochondria showed that the mito-ADH band could be produced from physiologically competent mitochondria by mechanical disruption or by treatment with detergents.The isozyme pattern was determined for the various physiological states of yeast growing anaerobically and aerobically on 2% glucose and aerobically on 2% ethanol, and for catabolite de-repressed cells undergoing an anaerobic → aerobic transition in continuous culture.The changing isozyme pattern substantiates the thesis that ADH-I is produced constitutively and that ADH-II is regulated via catabolite repression. It appears from the data that mito-ADH is more closely related to mitochondriogenesis than is ADH-II.

scholarly journals Identification and characterization of three genes that affect expression of ADH2 in Saccharomyces cerevisiae.

Genetics ◽  
1992 ◽  
Vol 132 (2) ◽  
pp. 351-359 ◽  
Author(s):  
L Karnitz ◽  
M Morrison ◽  
E T Young
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Alcohol Dehydrogenase ◽  
Glucose Repression ◽  
Isocitrate Lyase ◽  
Temperature Sensitive ◽  
Affect Expression ◽  
Dehydrogenase Isozyme ◽  
Selection Protocol ◽  
Identification And Characterization

Abstract Using a new selection protocol we have identified and preliminarily characterized three new loci (ADR7, ADR8 and ADR9) which affect ADH2 (alcohol dehydrogenase isozyme II) expression. Mutants were selected which activate ADH2 expression in the presence of an over-expressed, normally inactive ADR1 allele. The mutants had very similar phenotypes with the exception that one was temperature sensitive for growth. In the absence of any ADR1 allele, the mutants allowed ADH2 to partially escape glucose repression. However, unlike wildtype strains deleted for ADR1, the mutants were able to efficiently derepress ADH2. The mutations allowed a small escape from glucose repression for secreted invertase, but had no effect on the glucose repression of isocitrate lyase or malate dehydrogenase. The mutations were shown to be nonallelic to a wide variety of previously characterized mutations, including mutations that affect other glucose-repressed enzymes.

scholarly journals THE DISTRIBUTION OF LACTATE DEHYDROGENASE ISOZYMES IN HUMAN SKELETAL MUSCLE FIBERS

1964 ◽  
Vol 12 (8) ◽  
pp. 608-614 ◽  
Author(s):  
M. VAN WIJHE ◽  
M. C. BLANCHAER ◽  
S. ST. GEORGE-STUBBS
Keyword(s):  
Skeletal Muscle ◽  
Lactate Dehydrogenase ◽  
Human Skeletal Muscle ◽  
Muscle Fibers ◽  
Isozyme Pattern ◽  
Electrophoretic Separation ◽  
Lactate Dehydrogenase Isozymes ◽  
Dehydrogenase Isozyme ◽  
Lactate Dehydrogenase Isozyme ◽  
Normal Human

A study of the distribution of lactate dehydrogenase isozymes in single fibers from normal human skeletal muscle is presented. The fibers were classified into red, intermediate and white types on histochemical grounds and their lactate dehydrogenase isozyme content assessed by electrophoretic separation in veronal buffered agar. The results generally agreed with previous homogenate studies on animal skeletal muscle, in that the white fibers contained almost exclusively isozymes IV and V, whereas red fibers were rich in isozymes I, II and III, but IV and V also appeared indigenous to these fibers. The intermediate fibers had an isozyme pattern combining the features of red and white fibers. The metabolic implications of these findings are discussed.

Reptilian alcohol dehydrogenase: Isozyme divergence among submammalian vertebrates

1992 ◽  
Vol 11 (4) ◽  
pp. 412-412
Author(s):  
Lars Hjelmqvist ◽  
Jawed Shafqat ◽  
Hans Jörnvall
Keyword(s):  
Alcohol Dehydrogenase ◽  
Dehydrogenase Isozyme

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

Genetics ◽  
1987 ◽  
Vol 116 (4) ◽  
pp. 531-540
Author(s):  
Aileen K W Taguchi ◽  
Elton T Young
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Alcohol Dehydrogenase ◽  
Single Gene ◽  
Carbon Sources ◽  
Transcription Unit ◽  
Yeast Cells ◽  
Recessive Mutation ◽  
Yeast Saccharomyces Cerevisiae ◽  
Upstream Activating Sequence ◽  
A Site

ABSTRACT The alcohol dehydrogenase II (ADH2) gene of the yeast, Saccharomyces cerevisiae, is not transcribed during growth on fermentable carbon sources such as glucose. Growth of yeast cells in a medium containing only nonfermentable carbon sources leads to a marked increase or derepression of ADH2 expression. The recessive mutation, adr6-1, leads to an inability to fully derepress ADH2 expression and to an inability to sporulate. The ADR6 gene product appears to act directly or indirectly on ADH2 sequences 3' to or including the presumptive TATAA box. The upstream activating sequence (UAS) located 5' to the TATAA box is not required for the Adr6- phenotype. Here, we describe the isolation of a recombinant plasmid containing the wild-type ADR6 gene. ADR6 codes for a 4.4-kb RNA which is present during growth both on glucose and on nonfermentable carbon sources. Disruption of the ADR6 transcription unit led to viable cells with decreased ADHII activity and an inability to sporulate. This indicates that both phenotypes result from mutations within a single gene and that the adr6-1 allele was representative of mutations at this locus. The ADR6 gene mapped to the left arm of chromosome XVI at a site 18 centimorgans from the centromere.

Crystallization and Preliminary Crystallographic Studies of Saccharomyces cerevisiae Alcohol Dehydrogenase I

1994 ◽  
Vol 235 (2) ◽  
pp. 777-779 ◽  
Author(s):  
S. Ramaswamy ◽  
Darla Ann Kratzer ◽  
Andrew D. Hershey ◽  
Paul H. Rogers ◽  
Arthur Arnone ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Alcohol Dehydrogenase
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