Now at the Met: fine art of reversible sulfoxidation.
In this issue, Lee et al. (2013) exhibit methionine sulfoxidation in a new light. By bringing together two antagonistic enzymes affecting methionine redox state, the authors demonstrate that methionine oxidation constitutes a reversible, posttranslational regulatory mechanism, akin to protein phosphorylation.
Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel. Electronic address: tal.ilani@weizmann.ac.il.
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Deborah
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D000199:Actins / Q000378:metabolism*; D000818:Animals; D008264:Macrophages / Q000378:metabolism*; D008715:Methionine / Q000378:metabolism*; D051150:Methionine Sulfoxide Reductases / Q000235:genetics*; D008840:Microfilament Proteins; D008869:Microtubule-Associated Proteins / Q000378:metabolism*; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D010088:Oxidoreductases / Q000378:metabolism*
D000199:Actins; D008840:Microfilament Proteins; D008869:Microtubule-Associated Proteins; D008715:Methionine; C507541:Mical1 protein, mouse; D006899:Mixed Function Oxygenases; D010088:Oxidoreductases; D051150:Methionine Sulfoxide Reductases; C520510:Msrb2 protein, mouse