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

  • Wolfhard BANDLOW
  • , Gertrud STROBEL
  • , Cornelia ZOGLOWEK
  • , Ulrich OECHSNER
  • , Viktor MAGDOLEN
  • University of Munich
  • University of Ulm

Research output: Contribution to journalArticlepeer-review

43 Scopus citations

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.

Original languageEnglish
Pages (from-to)451-457
Number of pages7
JournalEuropean Journal of Biochemistry
Volume178
Issue number2
DOIs
StatePublished - Dec 1988
Externally publishedYes

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