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A new mutation for multiple drug resistance and modified plasma membrane ATPase activity in Schizosaccharomyces pombe

S Ulaszewski1, A Coddington, A Goffeau

  • 1Laboratoire d'Enzymologie, Université de Louvain, Louvain-La-Neuve, Belgium.

Current Genetics
|January 1, 1986
PubMed

Insights

A new mutation, pma1, in fission yeast confers resistance to positively charged compounds like Dio-9. This mutation affects plasma membrane ATPase activity and vanadate resistance.

Area of Science:

  • Molecular biology
  • Genetics
  • Biochemistry

Background:

  • The study investigates mutations affecting cellular transport and enzyme activity in Schizosaccharomyces pombe.
  • Previous research identified mutations cyh3 and cyh4 with similar resistance phenotypes.

Purpose of the Study:

  • To characterize a novel mutation, pma1, conferring resistance to specific compounds.
  • To understand the impact of pma1 on plasma membrane ATPase activity and vanadate sensitivity.

Main Methods:

  • Selection of mutant JV66 from wild-type S. pombe 972h- ade7-413 on Dio-9 containing medium.
  • Genetic analysis to identify and map the pma1 locus on chromosome I.
  • Biochemical assays to assess plasma membrane ATPase activity and vanadate resistance.

Main Results:

  • The pma1 mutation confers resistance to diguanidines and other positively charged compounds.
  • pma1 leads to decreased plasma membrane ATPase activity.
  • The mutation also confers resistance of the ATPase to vanadate.
  • The pma1 locus was mapped to chromosome I, distinct from previously described mutations.

Conclusions:

  • The pma1 mutation represents a new genetic locus in S. pombe with unique characteristics.
  • pma1 provides insights into the regulation of plasma membrane ATPase and transport mechanisms.

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