Abstract
In response to oxidative stress, cells activate numerous processes and initiate the expression of genes via redox-sensitive transcription factors including the multi sub-unit transcription factors nuclear factor-κB (NFκB), activator protein 1 (AP-1), Hypoxia-inducible factor 1 α (HIF1α), Polyoma virus enhancer-binding protein 2 (PEBP2), cAMP-responsive element-bindingprotein (CREB), Nuclear Factor I/CCAAT Transcription Factor (NFI/CTF), Nuclear transcription factor Y (NF-Y) and E4 Transcription Factor 1 - 60kDa (E4TF1-60). Thioredoxin plays a critical role in this by directly or indirectly (via redox factor 1) reducing redox-sensitive cysteine residues in these transcription factors to modify their tertiary structure, sub-cellular localisation,proteinprotein interactions or DNA-binding affinity. The identity of the redox-sensitive cysteine in E4TF1-60 has not been investigated so far. Determining which cysteines are redox-sensitive within the E4TF1-60 protein sequence together with elucidation of which property is modified will help to better understand the mechanism by which the E4TF1 complex is involved in regulating the cellular oxidative stress response.
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