Redox controls RecA protein activity via reversible oxidation of its methionine residues.
作者： Didier Vertommen , Frédéric Barras , Sindhu Chitteni-Pattu , Elizabeth A Wood , Josep Casadesús
DOI: 10.7554/ELIFE.63747
关键词:
摘要: Reactive oxygen species (ROS) cause damage to DNA and proteins. Here we report that the RecA recombinase is itself oxidized by ROS. Genetic biochemical analyses revealed oxidation of altered its repair recombination activities. Mass spectrometry analysis showed exposure ROS converted 4 out 9 Met residues methionine sulfoxide. Mimicking Met35 changing it for Gln caused complete loss function whereas mimicking Met164 resulted in constitutive SOS activation activity. Yet, all ROS-induced alterations activity were suppressed sulfoxide reductases MsrA MsrB. These findings indicate under oxidative stress, MsrA/B needed homeostasis control. The implication that, besides damaging structure directly, prevent hampering
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