Volume354,Number 1 (1998), in Article No. BB980671, “Cross-Linking and Disulfide Bond Formation of Introduced Cysteine Residues Suggest a Modified Model for the Tertiary Structure of URF13 in the Pore-Forming Oligomers,” by David M. Rhoads, Barbara Brunner-Neuenschwander, Charles S. Levings, III, and James N. Siedow, pages 158–164:

1998 ◽  
Vol 359 (2) ◽  
pp. 320
Keyword(s):  
Disulfide Bond ◽  
Tertiary Structure ◽  
Bond Formation ◽  
Cross Linking ◽  
Cysteine Residues ◽  
Disulfide Bond Formation ◽  
Modified Model

Two Critical Cysteine Residues Implicated in Disulfide Bond Formation and Proper Folding of Kir2.1

Biochemistry ◽  
2000 ◽  
Vol 39 (16) ◽  
pp. 4649-4657 ◽  
Author(s):  
Hee Cheol Cho ◽  
Robert G. Tsushima ◽  
The-Tin T. Nguyen ◽  
H. Robert Guy ◽  
Peter H. Backx
Keyword(s):  
Disulfide Bond ◽  
Bond Formation ◽  
Cysteine Residues ◽  
Disulfide Bond Formation

scholarly journals Regulation of the Yeast Yap1p Nuclear Export Signal Is Mediated by Redox Signal-Induced Reversible Disulfide Bond Formation

2001 ◽  
Vol 21 (18) ◽  
pp. 6139-6150 ◽  
Author(s):  
Shusuke Kuge ◽  
Minetaro Arita ◽  
Asako Murayama ◽  
Kazuhiro Maeta ◽  
Shingo Izawa ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Nuclear Localization ◽  
Disulfide Bond ◽  
Nuclear Export ◽  
Bond Formation ◽  
Nuclear Export Signal ◽  
Cysteine Residues ◽  
Disulfide Bond Formation ◽  
Disulfide Linkage ◽  
Export Signal

ABSTRACT Yap1p, a crucial transcription factor in the oxidative stress response of Saccharomyces cerevisiae, is transported in and out of the nucleus under nonstress conditions. The nuclear export step is specifically inhibited by H2O2 or the thiol oxidant diamide, resulting in Yap1p nuclear accumulation and induction of transcription of its target genes. Here we provide evidence for sensing of H2O2 and diamide mediated by disulfide bond formation in the C-terminal cysteine-rich region (c-CRD), which contains 3 conserved cysteines and the nuclear export signal (NES). The H2O2 or diamide-induced oxidation of the c-CRD in vivo correlates with induced Yap1p nuclear localization. Both were initiated within 1 min of application of oxidative stress, before the intracellular redox status of thioredoxin and glutathione was affected. The cysteine residues in the middle region of Yap1p (n-CRD) are required for prolonged nuclear localization of Yap1p in response to H2O2 and are thus also required for maximum transcriptional activity. Using mass spectrometry analysis, the H2O2-induced oxidation of the c-CRD in vitro was detected as an intramolecular disulfide linkage between the first (Cys598) and second (Cys620) cysteine residues; this linkage could be reduced by thioredoxin. In contrast, diamide induced each pair of disulfide linkage in the c-CRD, but in this case the cysteine residues in the n-CRD appeared to be dispensable for the response. Our data provide evidence for molecular mechanisms of redox signal sensing through the thiol-disulfide redox cycle coupled with the thioredoxin system in the Yap1p NES.

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