Large Mg(2+)-dependent currents are associated with the increased expression of ALR1 in Saccharomyces cerevisiae

FEMS Microbiol Lett. 2002 Aug 6;213(2):231-7. doi: 10.1111/j.1574-6968.2002.tb11311.x.

Abstract

Two genes in Saccharomyces cerevisiae, ALR1 and ALR2, encode proteins putatively involved in Mg(2+) uptake. The present study supports this role for ALR1 and provides the first electrophysiological characterisation of this protein. The patch-clamp technique was used to measure whole-cell ion currents in protoplasts prepared from the wild-type strain, the alr1 alr2 double mutant (CM66), and the double mutant over-expressing the ALR1 gene (CM66+ALR1). With 50 mM Mg(2+) in the bathing solution, the inward current in protoplasts of CM66+ALR1 averaged -264+/-48 pA at -150 mV. Inward currents measured in the wild-type and CM66 protoplasts were more than five-fold smaller. When Mg(2+) was the major cation in the pipette solution, time-dependent outward currents were also detected in CM66+ALR1 protoplasts suggesting ALR1 can facilitate Mg(2+) efflux as well as uptake. We conclude that the ALR1 gene encodes a transport protein. The large magnitude of the Mg(2+)-dependent currents suggests that ALR1 could function as a cation channel.

MeSH terms

  • Biological Transport
  • Carrier Proteins / biosynthesis*
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism
  • Cation Transport Proteins
  • Electrophysiology
  • Gene Expression
  • Ion Channels / physiology
  • Magnesium / metabolism*
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae / physiology
  • Saccharomyces cerevisiae Proteins / biosynthesis
  • Saccharomyces cerevisiae Proteins / genetics*

Substances

  • ALR1 protein, S cerevisiae
  • Carrier Proteins
  • Cation Transport Proteins
  • Ion Channels
  • Saccharomyces cerevisiae Proteins
  • Magnesium