Ycf1p attenuates basal level oxidative stress response in Saccharomyces cerevisiae

FEBS Lett. 2012 Mar 23;586(6):847-53. doi: 10.1016/j.febslet.2012.02.010. Epub 2012 Feb 23.

Abstract

Ycf1p function is regulated by casein kinase 2α, Cka1p, via phosphorylation of Ser251. Cka1p-mediated phosphorylation of Ycf1p is attenuated in response to high salt stress. Previous results from our lab suggest a role for Ycf1p in cellular resistance to salt stress. Here, we show that Ycf1p plays an important role in cellular resistance to salt stress by maintaining the cellular redox balance via glutathione recycling. Our results suggest that during acute salt stress increased Sod1p, Sod2p and Ctt1p activity is the main compensatory for the loss in Ycf1p function that results from reduced Ycf1p-dependent recycling of cellular GSH levels.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • ATP-Binding Cassette Transporters / genetics
  • ATP-Binding Cassette Transporters / metabolism*
  • Animals
  • Biomarkers / metabolism
  • Casein Kinase II / metabolism
  • Glutathione / metabolism
  • Hydrogen Peroxide / pharmacology
  • Oxidants / pharmacology
  • Oxidation-Reduction
  • Oxidative Stress*
  • Phosphorylation
  • Saccharomyces cerevisiae / drug effects
  • Saccharomyces cerevisiae / physiology*
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Salts / pharmacology*
  • Superoxide Dismutase / genetics
  • Superoxide Dismutase / metabolism
  • Superoxide Dismutase-1

Substances

  • ATP-Binding Cassette Transporters
  • Biomarkers
  • Oxidants
  • Saccharomyces cerevisiae Proteins
  • Salts
  • YCF1 protein, S cerevisiae
  • Hydrogen Peroxide
  • Superoxide Dismutase
  • Superoxide Dismutase-1
  • superoxide dismutase 2
  • Casein Kinase II
  • Glutathione