1887

Abstract

This study aims to define the cellular roles of methionine sulfoxide reductases A and B, evolutionarily highly conserved enzymes able to repair oxidized methionines in proteins. and mutants were exposed to an internal oxidative stress by growing them under aerobic conditions on glycerol. Interestingly, the mutants behave completely differently under these conditions. The mutant is inhibited, whereas the mutant is stimulated in its growth in comparison with the parent strain. Glycerol can be catabolized by either the GlpK or DhaK pathways in . Our results strongly suggest that in the mutant, glycerol is catabolized via the GlpK pathway leading to increased synthesis of HO, which accumulates to concentrations inhibitory to growth in comparison with the parent strain. In contrast in the mutant, glycerol is metabolized via the DhaK pathway which is not accompanied by the synthesis of HO. The molecular basis for the differences in glycerol flux seems to be due to expression differences of the two glycerol-catabolic operons in the mutants.

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/content/journal/micro/10.1099/mic.0.065037-0
2013-03-01
2021-07-30
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