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Repairing oxidized proteins in the bacterial envelope using respiratory chain electrons

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Gennaris, Alexandra [UCL] Ezraty, Benjamin Henry, Camille Agrebi, Rym Vergnes, Alexandra Leverrier, Pauline [UCL] Szewczyk, Joanna [UCL] Vertommen, Didier [UCL] Collet, Jean-François [UCL] Barras, Frédéric

The reactive species of oxygen and chlorine damage cellular components, potentially leading to cell death. In proteins, the sulfur-containing amino acid methionine is converted to methionine sulfoxide, which can cause a loss of biological activity. To rescue proteins with methionine sulfoxide residues, living cells express methionine sulfoxide reductases (Msrs) in most subcellular compartments, including the cytosol, mitochondria and chloroplasts. Here we report the identification of an enzymatic system, MsrPQ, repairing proteins containing methionine sulfoxide in the bacterial cell envelope, a compartment particularly exposed to the reactive species of oxygen and chlorine generated by the host defence mechanisms. MsrP, a molybdo-enzyme, and MsrQ, a haem-binding membrane protein, are widely conserved throughout Gram-negative bacteria, including major human pathogens. MsrPQ synthesis is induced by hypochlorous acid, a powerful antimicrobial released by neutrophils. Consistently, MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA. For this activity, MsrPQ uses electrons from the respiratory chain, which represents a novel mechanism to import reducing equivalents into the bacterial cell envelope. A remarkable feature of MsrPQ is its capacity to reduce both rectus (R-) and sinister (S-) diastereoisomers of methionine sulfoxide, making this oxidoreductase complex functionally different from previously identified Msrs. The discovery that a large class of bacteria contain a single, non-stereospecific enzymatic complex fully protecting methionine residues from oxidation should prompt a search for similar systems in eukaryotic subcellular oxidizing compartments, including the endoplasmic reticulum.

Document type Article de périodique (Journal article) – Article de recherche
Publication date 2015
Language Anglais
Journal information "Nature : international weekly journal of science" - Vol. 528, no.7582, p. 409-412 (2015)
Peer reviewed yes
Publisher Nature Publishing Group (London)
issn 0028-0836
e-issn 1476-4687
Publication status Publié
Affiliation UCL - SSS/DDUV - Institut de Duve
Links
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Bibliographic reference Gennaris, Alexandra ; Ezraty, Benjamin ; Henry, Camille ; Agrebi, Rym ; Vergnes, Alexandra ; et. al. Repairing oxidized proteins in the bacterial envelope using respiratory chain electrons. In: Nature : international weekly journal of science, Vol. 528, no.7582, p. 409-412 (2015)
Permanent URL http://hdl.handle.net/2078.1/168128