1sse
From Proteopedia
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Solution structure of the oxidized form of the Yap1 redox domain
Overview
The ability of organisms to alter their gene expression patterns in, response to environmental changes is essential for viability. A central, regulator of the response to oxidative stress in Saccharomyces cerevisiae, is the Yap1 transcription factor. Upon activation by increased levels of, reactive oxygen species, Yap1 rapidly redistributes to the nucleus where, it regulates the expression of up to 70 genes. Here we identify a, redox-regulated domain of Yap1 and determine its high-resolution solution, structure. In the active oxidized form, a nuclear export signal (NES) in, the carboxy-terminal cysteine-rich domain is masked by, disulphide-bond-mediated interactions with a conserved amino-terminal, alpha-helix. Point mutations that weaken the hydrophobic interactions, between the N-terminal alpha-helix and the C-terminal NES-containing, domain abolished redox-regulated changes in subcellular localization of, Yap1. Upon reduction of the disulphide bonds, Yap1 undergoes a change to, an unstructured conformation that exposes the NES and allows, redistribution to the cytoplasm. These results reveal the structural basis, of redox-dependent Yap1 localization and provide a previously unknown, mechanism of transcription factor regulation by reversible intramolecular, disulphide bond formation.
About this Structure
1SSE is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structural basis for redox regulation of Yap1 transcription factor localization., Wood MJ, Storz G, Tjandra N, Nature. 2004 Aug 19;430(7002):917-21. PMID:15318225
Page seeded by OCA on Wed Nov 21 02:37:35 2007
