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Journal of Bacteriology, October 2008, p. 6609-6614, Vol. 190, No. 20
0021-9193/08/$08.00+0 doi:10.1128/JB.00588-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Laboratoire de Chimie Bactérienne, Université de la Méditerranée, UPR 9043-CNRS, 31, Chemin Joseph Aiguier, 13402 Marseille, France,1 Service de spectrométrie de masse, 31, Chemin Joseph Aiguier, 13402 Marseille, France2
Received 29 April 2008/ Accepted 31 July 2008
Carbonylation is currently used as a marker for irreversible protein oxidative damage. Several studies indicate that carbonylated proteins are more prone to degradation than their nonoxidized counterparts. In this study, we observed that in Escherichia coli, more than 95% of the total carbonyl content consisted of insoluble protein and most were cytosolic proteins. We thereby demonstrate that, in vivo, carbonylated proteins are detectable mainly in an aggregate state. Finally, we show that detectable carbonylated proteins are not degraded in vivo. Here we propose that some carbonylated proteins escape degradation in vivo by forming carbonylated protein aggregates and thus becoming nondegradable. In light of these findings, we provide evidence that the accumulation of nondegradable carbonylated protein presented in an aggregate state contributes to the increases in carbonyl content observed during senescence.
Published ahead of print on 8 August 2008.
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