Open AccessCharacterization of Saccharomyces cerevisiae mutants lacking the E1α subunit of the pyruvate dehydrogenase complex
Author(s) -
WENZEL Thibaut J.,
BERG Marco A.,
VISSER Wiebe,
BERG Johan A.,
STEENSMA H. Yde
Publication year - 1992
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1992.tb17338.x
Subject(s) - pyruvate dehydrogenase complex , pyruvate dehydrogenase phosphatase , protein subunit , mutant , pyruvate dehydrogenase kinase , saccharomyces cerevisiae , pyruvate dehydrogenase lipoamide kinase isozyme 1 , biochemistry , branched chain alpha keto acid dehydrogenase complex , pyruvate decarboxylation , gene , oxoglutarate dehydrogenase complex , biology , dihydrolipoyl transacetylase , dehydrogenase , microbiology and biotechnology , enzyme
Pyruvate dehydrogenase mutants of Saccharomyces cerevisiae were isolated by disruption of the PDAl gene. To this end, the PDAl gene encoding the E1α subunit of the pyruvate dehydrogenase complex was replaced by the dominant Tn5ble marker. Disruption of the PDAl gene abolished production of the E1α subunit and pyruvate dehydrogenase activity. Two additional phenotypes were observed in the Pdh − mutants: (a) a reduced growth rate in glucose medium which was partially complemented by the amino acid leucine; (b) an increase in formation of petites which lack mitochondrial DNA [rho°], during growth on glucose. Both phenotypes were shown to be a result of inactivation of the PDAl gene. Explanations for these phenotypes are discussed.