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Journal of Bacteriology, February 2008, p. 887-893, Vol. 190, No. 3
0021-9193/08/$08.00+0 doi:10.1128/JB.01603-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.
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Laetitia Fraysse,1,
Danielle Moinier,2 and
Sam Dukan1*
Laboratoire de Chimie Bactérienne-UPR 9043-CNRS/Université de la Méditerranée, 31, Chemin Joseph Aiguier, 13402, Marseille, France,1 Service de spectrométrie de masse/CNRS/31, Chemin Joseph Aiguier, 13402 Marseille, France2
Received 3 October 2007/ Accepted 9 November 2007
Protein aggregation is a phenomenon observed in all organisms and has often been linked with cell disorders. In addition, several groups have reported a virtual absence of protein aggregates in healthy cells. In contrast to previous studies and the expected outcome, we observed aggregated proteins in aerobic exponentially growing and "healthy" Escherichia coli cells. We observed overrepresentation of "aberrant proteins," as well as substrates of the major conserved chaperone DnaK (Hsp70) and the protease ClpXP (a serine protease), in the aggregates. In addition, the protein aggregates appeared to interact with chaperones known to be involved in the aggregate repair pathway, including ClpB, GroEL, GroES, and DnaK. Finally, we showed that the levels of reactive oxygen species and unfolded or misfolded proteins determine the levels of protein aggregates. Our results led us to speculate that protein aggregates may function as a temporary "trash organelle" for cellular detoxification.
Published ahead of print on 26 November 2007.
Supplemental material for this article may be found at http://jb.asm.org/.
E.M. and L.F. contributed equally to this work.
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