Linked Life Data

392242

Source:http://linkedlifedata.com/resource/pubmed/id/392242

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1980-3-27
pubmed:abstractText
Starting with yeast cells lacking the constitutive alcohol dehydrogenase activity (ADHI), mutants with partially glucose-insensitive formation of ADHII were isolated. Genetic analysis showed that four mutants (designated ADR3c) were linked to the ADHII-structural gene, ADR2, and were cis-dominant. On derepression, two of them produced elevated ADHII-levels, indicating a promotor function of the altered controlling site. The other ADR3c-mutant alleles affected the ADHII-subunit association in diploids carrying two electrophoretically distinct alleles of the structural gene ADR2. Twelve semidominant constitutive mutants could be attributed to gene ADR1 (ADR1c-alleles) previously identified by recessive mutants with blocked derepression. This suggested a positive regulatory role of the ADR1 gene product on the expression of the ADHII-structural gene. A pleiotropic mutation ccr1 (Ciriacy, 1977) was epistatic over glucose-resistant ADHII-formation caused by ADR1c-alleles. From this it was concluded that CCR1 specifies for a product co-activating the structural gene or modifying the ADR1-gene product. A further regulatory element (gene designation ADR4) not linked to the structural gene could be identified upon isolation of recessive constitutive mutants adr4 from a ccr1 ADR1c-double mutant.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0026-8925
pubmed:author
pubmed:issnType
Print
pubmed:volume
176
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
427-31
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Isolation and characterization of further cis- and trans-acting regulatory elements involved in the synthesis of glucose-repressible alcohol dehydrogenase (ADHII) in Saccharomyces cerevisiae.
pubmed:publicationType
Journal Article