Laboratoire de Chimie Bactérienne UMR 7283



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Oxidative stress damage and repair in enterobacteriaceae

Our team aims at deciphering oxidative stress responses using Escherichia coli as a model bacterium and Salmonella enterica as pathogen bacterium. Proteins can be targeted and damaged by reactive oxygen species (ROS). Among all amino acids, methionine is the most sensitive residue to ROS, which can be converted to methionine sulfoxide (Met-SO). To rescue Met-SO containing proteins, living organisms synthesize methionine sulfoxide reductases (Msr). Enterobacteriaceae contains two cytosolic Msr (MsrA, MsrB) and one periplasmic Msr (MsrP). In addition, two other Msr (MsrC and BisC) are present in the cytoplasm where they can reduce only free Met-SO. The identification of protein targets and cellular processes under the surveillance of Msr is in progress. Our studies, both at the molecular and cellular levels, are orientated towards understanding of the contribution of each Msr in oxidative stress resistance, especially during bleach stress.