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Escherichia coli heat-shock proteins IbpA/B are involved in resistance to oxidative stress induced by copper

Dorota Kuczyska-Winik

Department of Biochemistry, University of Gdask, Kadki 24, 80-952 Gdask, Poland

Correspondence
Ewa Laskowska
lasko{at}biotech.ug.gda.pl

The small heat-shock proteins IbpA/B are molecular chaperones that bind denatured proteins and facilitate their subsequent refolding by the ATP-dependent chaperones DnaK, DnaJ, GrpE and ClpB. In this report, we demonstrate that IbpA/B participate in the defence against copper-induced stress under aerobic conditions. In the presence of oxygen, ibpA/B cells exhibit increased sensitivity to copper ions and accumulate elevated amounts of oxidized proteins, while under oxygen depletion, the ibpA/B mutation has no effect on copper tolerance. This indicates that IbpA/B protect Escherichia coli cells from oxidative damage caused by copper. We show that AdhE, one of the proteins exposed to oxidation, is protected by IbpA/B against copper-mediated inactivation both in vivo and in vitro.