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RulesGoverningSelectiveProteinCarbonylation
EtienneMaisonneuve1.,AdrienDucret1.,PierreKhoueiry1,SabrinaLignon2,SoniaLonghi3 ,Emmanuel
Talla1*,SamDukan1*
1Laboratoire de Chimie Bacte′rienne – Aix Marseille Universite′ - UPR 9043-CNRS, 31, Chemin Joseph Aiguier, Marseille, France, 2Service de micro se′quenc?age et de
spectrome′triedemasse–CNRS-31,CheminJosephAiguier,Marseille,France,3ArchitectureetFonctiondesMacromole′culesBiologiques,AixMarseilleUniversite′-CNRS,
UMR6098,Marseille,France
Abstract
Background:Carbonylderivativesaremainlyformedbydirectmetal-catalysedoxidation(MCO)attacksontheamino-acidside
chainsofproline,arginine,lysineandthreonineresidues.Forreasonsunknown,onlysomeproteinsarepronetocarbonylation.
Methodology/Principal Findings: We used mass spectrometry analysis to identify carbonylated sites in: BSA that had
undergoneinvitroMCO,and23carbonylatedproteinsinEscherichiacoli.Thepresenceofacarbonylatedsiterenderedthe
neighbouringcarbonylatablesitemorepronetocarbonylation.Mostcarbonylatedsiteswerepresentwithinhotspotsof
carbonylation.Theseobservationsledustosuggestrulesforidentifyingsitesmorepronetocarbonylation.Weusedthese
rules to design an in silico model (available at rs-mrs.fr/CSPD/), allowing an effective and accurate
predictionofsitesandofproteinsmorepronetocarbonylationintheE.coliproteome.
Conclusions/Significance: Weobservedthatproteinsevolvetoeitherselectivelymaintainorlosepredictedhotspotsof
carbonylation depending on their biological function. As our predictive model also allows efficient detection of
carbonylatedproteinsinBacillussubtilis,webelievethatourmodelmaybeextendedtodirectMCOattacksinallorganisms.
Citation: Maisonneuve E, Ducret A, Khoueiry P, Lignon S, Longhi S, et al. (2009) Rules Governing Selective Protein Carbonylation. PLoS ONE 4(10): e7269.
doi:10.1371/journal.pone.0007269
Editor:AndreasHofmann,GriffithUniversity,Australia
ReceivedJune29,2009;AcceptedJuly28,2009;PublishedOctober5,2009
Copyright:?2009Maisonneuveetal.Thisisanope
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