Journal
FEBS LETTERS
Volume 589, Issue 6, Pages 718-725Publisher
WILEY-BLACKWELL
DOI: 10.1016/j.febslet.2015.01.039
Keywords
AtHSFA8; Fluorescence resonance energy transfer; Heat stress transcription factor; Redox-regulation; Cytoplasmic-nuclear shuttling; Reactive oxygen species
Funding
- DFG [SFB613, D12, Di 346, SPP1710]
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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. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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