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J Biol Chem, Vol. 274, Issue 37, 26027-26032, September 10, 1999
From the Department of Cell and Molecular Biology-Microbiology,
Göteborg University, Box 462, 405 30 Göteborg, Sweden
and the Department of Microbiology, Lund University, Lund 223 62, Sweden
Analysis of protein carbonylation demonstrates
that the stasis-induced catalases and cytoplasmic superoxide dismutases
(SOD) have a role in preventing accelerated protein oxidation during growth arrest of Escherichia coli cells. A larger number of
proteins are carbonylated in cells lacking cytoplasmic SOD
compared with cells lacking catalases, OxyR, or RpoS which,
in turn, exhibit a larger number of oxidized proteins than the
wild-type parent. Proteins exclusively oxidized during stasis in
mutants lacking cytoplasmic SOD include GroEL, EF-G, and the acidic
isoform of H-NS indicating that these mutants experience problems in
peptide elongation and maintaining protein and DNA architecture. These mutants also survive stasis poorly. Likewise, but to a much lesser extent, mutations in oxyR, an oxidative stress regulator,
shorten the life-span of stationary phase cells. The low plating
efficiency of cells lacking OxyR is the result of their inability to
grow on standard culture plates unless plating is performed
anaerobically or with high concentration of catalase. In contrast,
cells lacking cytoplasmic SOD appear to die prior to plating. Our data
points to the importance of oxidative stress defense in stasis
survival, and we also demonstrate that the life-span of growth-arrested wild-type E. coli cells can be significantly extended by
omitting oxygen.
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