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Published 4 December 2006. doi:10.1083/jcb.200606005
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 175, Number 5, 779-789
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Article

 Oxidation state governs structural transitions in peroxiredoxin II that correlate with cell cycle arrest and recovery

Timothy J. Phalen1, Kelly Weirather1, Paula B. Deming2, Vikas Anathy1, Alan K. Howe2, Albert van der Vliet1, Thomas J. Jönsson3, Leslie B. Poole3, and Nicholas H. Heintz1

1 Department of Pathology and 2 Department of Pharmacology, University of Vermont College of Medicine, Burlington, VT 05405
3 Center for Structural Biology, Wake Forest University School of Medicine, Winston-Salem, NC 27157

Correspondence to Nicholas H. Heintz: nicholas.heintz{at}uvm.edu

Inactivation of eukaryotic 2-Cys peroxiredoxins (Prxs) by hyperoxidation has been proposed to promote accumulation of hydrogen peroxide (H2O2) for redox-dependent signaling events. We examined the oxidation and oligomeric states of PrxI and -II in epithelial cells during mitogenic signaling and in response to fluxes of H2O2. During normal mitogenic signaling, hyperoxidation of PrxI and -II was not detected. In contrast, H2O2-dependent cell cycle arrest was correlated with hyperoxidation of PrxII, which resulted in quantitative recruitment of ~66- and ~140-kD PrxII complexes into large filamentous oligomers. Expression of cyclin D1 and cell proliferation did not resume until PrxII-SO2H was reduced and native PrxII complexes were regenerated. Ectopic expression of PrxI or -II increased Prx-SO2H levels in response to oxidant exposure and failed to protect cells from arrest. We propose a model in which Prxs function as peroxide dosimeters in subcellular processes that involve redox cycling, with hyperoxidation controlling structural transitions that alert cells of perturbations in peroxide homeostasis.

Abbreviations used in this paper: DNCB, 1-chloro-2,4-dinitrobenzene; ERK, extracellular signal–related kinase; GOx, glucose oxidase; GSH, glutathione; HMC, high molecular mass complex; Prx, peroxiredoxin; ROS, reactive oxygen species; Trx, thioredoxin; TrxR, thioredoxin reductase.


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