The S. cerevisiae Yap1 and Yap2 transcription factors share a common cadmium-sensing domain

FEBS Lett. 2007 Jan 23;581(2):187-95. doi: 10.1016/j.febslet.2006.11.083. Epub 2006 Dec 13.

Abstract

Towards elucidating the function of Yap2, which remains unclear, we have taken advantage of the C-terminal homology between Yap1 and Yap2. Swapping domains experiments show that the Yap2 C-terminal domain functionally substitutes for the homologous Yap1 domain in the response to Cd, but not to H2O2. We conclude that specificity determinants of the Cd response are encoded within both Yap1 and Yap2 C-terminus, whereas those required for H2O2 response are only present in the Yap1 C-terminus. Furthermore, our results identify FRM2 as Cd-responsive Yap2 target and indicate a possible role of this protein in regulating a metal stress response.

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Cadmium / metabolism*
  • Cadmium / toxicity
  • Cysteine / chemistry
  • Cysteine / genetics
  • Hydrogen Peroxide / metabolism
  • Hydrogen Peroxide / toxicity
  • Karyopherins / metabolism
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Receptors, Cytoplasmic and Nuclear / metabolism
  • Saccharomyces cerevisiae / drug effects
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Transcription Factors / chemistry
  • Transcription Factors / genetics
  • Transcription Factors / metabolism*
  • Transcriptional Activation

Substances

  • CAD1 protein, S cerevisiae
  • Karyopherins
  • Receptors, Cytoplasmic and Nuclear
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • YAP1 protein, S cerevisiae
  • exportin 1 protein
  • Cadmium
  • Hydrogen Peroxide
  • Cysteine