Is overoxidation of peroxiredoxin physiologically significant?
Eukaryotic peroxiredoxins are highly susceptible to sulfinic acid formation. This overoxidation, which is thought to convert peroxiredoxins into chaperones, can be reversed by sulfiredoxins. Several organisms, including Caenorhabditis elegans, lack sulfiredoxins but encode sestrins, proteins proposed to be functionally equivalent. We induced peroxiredoxin overoxidation in C. elegans with a short peroxide pulse. We found that reduction of overoxidized peroxiredoxin 2 (PRDX-2) was extremely slow and sestrin-independent, strongly implying that worms lack an efficient repair system. Analysis of PRDX-2's overoxidation status during C. elegans lifespan revealed no accumulation of overoxidized PRDX-2 at any point, questioning whether PRDX-2 overoxidation in worms is physiologically relevant.
Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109, USA.
Maike
M
Thamsen
Caroline
C
Kumsta
Fei
F
Li
Ursula
U
Jakob
D000818:Animals; D017173:Caenorhabditis elegans / Q000187:drug effects / Q000378:metabolism; D029742:Caenorhabditis elegans Proteins / Q000378:metabolism*; D006801:Humans; D010084:Oxidation-Reduction / Q000187:drug effects; D010545:Peroxides / Q000494:pharmacology; D054464:Peroxiredoxins / Q000378:metabolism*
D029742:Caenorhabditis elegans Proteins; D010545:Peroxides; C534226:PRDX-2 protein, C elegans; D054464:Peroxiredoxins