Journal
SCIENCE
Volume 300, Issue 5619, Pages 650-653Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1080405
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Funding
- NIEHS NIH HHS [ES00210] Funding Source: Medline
- NIGMS NIH HHS [GM50389, R01 GM050389-10, R01 GM050389] Funding Source: Medline
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Eukaryotic 2-Cys peroxiredoxins (2-Cys Prxs) not only act as antioxidants, but also appear to regulate hydrogen peroxide-mediated signal transduction. We show that bacterial 2-Cys Prxs are much less sensitive to oxidative inactivation than are eukaryotic 2-Cys Prxs. By identifying two sequence motifs unique to the sensitive 2-Cys Prxs and comparing the crystal structure of a bacterial 2-Cys Prx at 2.2 angstrom resolution with other Prx structures, we define the structural origins of sensitivity. We suggest this adaptation allows 2-Cys Prxs to act as floodgates, keeping resting levels of hydrogen peroxide low, while permitting higher levels during signal transduction.
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