rules governing selective protein carbonylation规则选择蛋白质羰基化.pdfVIP

Rules Governing Selective Protein Carbonylation 1. 1. 1 2 3 Etienne Maisonneuve , Adrien Ducret , Pierre Khoueiry , Sabrina Lignon , Sonia Longhi , Emmanuel 1 1 Talla *, Sam Dukan * ´ ´ ´ 1 Laboratoire de Chimie Bacterienne – Aix Marseille Universite - UPR 9043-CNRS, 31, Chemin Joseph Aiguier, Marseille, France, 2 Service de micro sequenc¸age et de ´ ´ ´ spectrometrie de masse – CNRS-31, Chemin Joseph Aiguier, Marseille, France, 3 Architecture et Fonction des Macromolecules Biologiques, Aix Marseille Universite - CNRS, UMR 6098, Marseille, France Abstract Background: Carbonyl derivatives are mainly formed by direct metal-catalysed oxidation (MCO) attacks on the amino-acid side chains of proline, arginine, lysine and threonine residues. For reasons unknown, only some proteins are prone to carbonylation. Methodology/Principal Findings: We used mass spectrometry analysis to identify carbonylated sites in: BSA that had undergone in vitro MCO, and 23 carbonylated proteins in Escherichia coli. The presence of a carbonylated site rendered the neighbouring carbonylatable site more prone to carbonylation. Most carbonylated sites were present within hot spots of carbonylation. These observations led us to suggest rules for identifying sites more prone to carbonylation. We used these rules to design an in silico model (available at rs-mrs.fr/CSPD/),