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PMID: 2850178 Published · ppublish English Journal Article

Yeast adenylate kinase is active simultaneously in mitochondria and cytoplasm and is required for non-fermentative growth.

European journal of biochemistry ·Vol. 178 ·No. 2 ·1988-12-15 ·Pages 451-7

Bandlow W, Strobel G, Zoglowek C, Oechsner U, Magdolen V

Abstract

Displacement of the single copy structural gene for yeast adenylate kinase (long version) by a disrupted nonfunctional allele is tolerated in haploid cells. Since adenylate kinase activity is a pre-requisite for cell viability, the survival of haploid disruption mutants is indicative of the presence of an adenylate kinase isozyme in yeast, capable of forming ADP from AMP and, thus, of complementing the disrupted allele. The phenotype of these disruption mutants is pet, showing that complementation occurs only under fermentative conditions. Even on glucose, growth of the disruption mutants is slow. Adenylate kinase activity is found both in mitochondria and cytoplasm of wild type yeast. The disruption completely destroys the activity in mitochondria, whereas in the cytoplasmic fraction about 10% is retained. An antibody raised against yeast mitochondrial adenylate kinase recognizes cross-reacting material both in mitochondria and cytoplasm of the wild type, but fails to do so in each of the respective mutant fractions. The data indicate that yeast adenylate kinase (long version, AKY2) simultaneously occurs and is active in mitochondria and cytoplasm of the wild type. Nevertheless, it lacks a cleavable pre-sequence for import into mitochondria. A second, minor isozyme, encoded by a separate gene, is present exclusively in the cytoplasm.

MeSH Terms
Adenosine Diphosphate/biosynthesis Adenosine Monophosphate/biosynthesis Adenylate Kinase/genetics,metabolism Cytoplasm/enzymology Fermentation Isoenzymes/genetics,metabolism Mitochondria/enzymology Mutation Oxidation-Reduction Phosphotransferases/metabolism Plasmids Restriction Mapping Saccharomyces cerevisiae/enzymology Subcellular Fractions/enzymology
Chemicals
Isoenzymes Adenosine Monophosphate Adenosine Diphosphate Phosphotransferases Adenylate Kinase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Bandlow W
Institute for Genetics and Microbiology, University of Munich, Federal Republic of Germany.
Strobel G
Zoglowek C
Oechsner U
Magdolen V
Article Info
Journal
European journal of biochemistry
Abbr.
Eur J Biochem
ISSN
0014-2956
Published
1988-12-15
Pages
451-7
Language
English
Region
England
NLM ID
0107600
Subset
IM
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