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Reference: Okazaki S, et al. (2007) Multistep disulfide bond formation in Yap1 is required for sensing and transduction of H(2)O(2) stress signal. Mol Cell 27(4):675-88

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Abstract


Redox reactions involving cysteine thiol-disulfide exchange are crucial for sensing intracellular levels of H(2)O(2). However, oxidation-sensitive dithiols are also sensitive to intracellular reducing agents, and disulfide bonds are thus transient. The yeast transcription factor Yap1 is activated by disulfide-induced structural changes in the nuclear export signal in a carboxy-terminal domain. We show herein that the activation of Yap1 by H(2)O(2) requires multistep formation of disulfide bonds. One disulfide bond forms within 15 s in an amino-terminal domain, and then disulfide bonds linking the two domains accumulate. The multiple interdomain disulfide bonds, which result in reduction-resistant Yap1, are required for transduction of the H(2)O(2) stress signal to induce the appropriate level and duration of specific transcription. Our results suggest both a mechanism wherein the H(2)O(2) levels might be sensed by Yap1 and the way in which the NADPH levels might be maintained by altering the redox status of Yap1.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Okazaki S, Tachibana T, Naganuma A, Mano N, Kuge S
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