Redox-dependent translocation of the heat shock transcription factor AtHSFA8 from the cytosol to the nucleus in Arabidopsis thaliana

FEBS Lett. 2015 Mar 12;589(6):718-25. doi: 10.1016/j.febslet.2015.01.039. Epub 2015 Feb 7.

Abstract

The hypothesis is tested that some heat stress transcription factors (HSFs) are activated after formation of inter- or intramolecular disulfide bonds. Based on in silico analyses we identified conserved cysteinyl residues in AtHSFA8 that might function as redox sensors in plants. AtHSFA8 represents a redox-sensitive transcription factor since upon treatment of protoplasts with H2O2 YFP-labeled HSFA8 was translocated to the nucleus in a time-dependent manner. Site-directed mutagenesis of the conserved residues Cys24 and Cys269 blocked translocation of HSFA8 to the nucleus. The findings concur with a model where HSFA8 functions as redox sensing transcription factor within the stress-responsive transcriptional network.

Keywords: AtHSFA8; Cytoplasmic-nuclear shuttling; Fluorescence resonance energy transfer; Heat stress transcription factor; Reactive oxygen species; Redox-regulation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Arabidopsis / cytology
  • Arabidopsis / metabolism*
  • Arabidopsis Proteins / chemistry
  • Arabidopsis Proteins / metabolism*
  • Cell Nucleus / metabolism*
  • Conserved Sequence
  • Cytosol / metabolism
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism*
  • Heat Shock Transcription Factors
  • Hydrogen Peroxide / metabolism
  • Molecular Sequence Data
  • Oxidation-Reduction
  • Protein Transport
  • Transcription Factors / chemistry
  • Transcription Factors / metabolism*

Substances

  • Arabidopsis Proteins
  • DNA-Binding Proteins
  • HSFA8 protein, Arabidopsis
  • Heat Shock Transcription Factors
  • Transcription Factors
  • Hydrogen Peroxide