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J Biol Chem, Vol. 273, Issue 5, 3027-3032, January 30, 1998
From the Departament de Ciències Mèdiques
Bàsiques, Facultat de Medicina, Universitat de Lleida, 25198 Lleida, Spain
In the present study we have analyzed protein
oxidation on Escherichia coli when these cells were
submitted to different stress conditions such as hydrogen peroxide,
superoxide-generating compounds, and iron overloading. Carbonyl groups
on oxidized cell proteins were examined by Western blot immunoassay.
When anaerobically grown E. coli cells were exposed to
hydrogen peroxide stress, alcohol dehydrogenase E, elongation factor G,
the heat shock protein DNA K, oligopeptide-binding protein A, enolase,
and the outer membrane protein A were identified as the major protein
targets. A similar immunostained band pattern was found when cells were shifted from anaerobic to aerobic conditions in the presence of different concentrations of iron; it is relevant to note that oxidation
of outer membrane protein C, not observed in peroxide stress
conditions, was clearly detected as the concentration of iron was
increased in the culture media. The hydrogen peroxide stress performed
under aerobic conditions affected the
Identification of the Major Oxidatively Damaged Proteins in
Escherichia coli Cells Exposed to Oxidative Stress
-subunit of
F0F1-ATPase; the rest of the oxidized protein
pattern was very similar to that found for anaerobic conditions, with
the exception of alcohol dehydrogenase E, a protein not synthesized
aerobically. Cells submitted to superoxide stress using menadione
showed a more specific pattern in which elongation factor G and the
-subunit of F0F1-ATPase were affected
significantly. When paraquat was used, although the degree of oxidative
damage was lower, the same two modified proteins were detected, and DNA
K was also clearly damaged. Cell viability was affected to different
extents depending on the type of stress exerted. The results described
in this paper provide data about the in vivo effects of
oxidative stress on protein oxidation and give insights into
understanding how such modifications can affect cellular functions.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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