Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109, USA.
Antioxid Redox Signal. 2011 Feb 15;14(4):725-30. doi: 10.1089/ars.2010.3717. Epub 2010 Dec 17.
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.
真核过氧化物酶极易形成亚磺酸。这种过氧化被认为将过氧化物酶转化为伴侣蛋白，可被硫氧还蛋白逆转。包括秀丽隐杆线虫在内的几种生物缺乏硫氧还蛋白，但编码 sestrins，这种蛋白被认为具有功能等效性。我们用短暂的过氧化物脉冲诱导秀丽隐杆线虫过氧化物酶的过氧化。我们发现，过氧化的过氧化物酶 2（PRDX-2）的还原非常缓慢且不依赖 sestrins，这强烈表明蠕虫缺乏有效的修复系统。在秀丽隐杆线虫的寿命过程中对 PRDX-2 的过氧化状态进行分析，发现任何时候都没有过氧化 PRDX-2 的积累，这质疑了蠕虫中 PRDX-2 的过氧化是否在生理上相关。
