Proline Metabolism IncreaseskatGExpression and Oxidative Stress Resistance in Escherichia coli

Proline dehydrogenase Regulon
DOI: 10.1128/jb.02282-14 Publication Date: 2014-11-11T05:10:25Z
ABSTRACT
The oxidation of l -proline to glutamate in Gram-negative bacteria is catalyzed by the proline utilization A (PutA) flavoenzyme, which contains dehydrogenase (PRODH) and Δ 1 -pyrroline-5-carboxylate (P5C) domains a single polypeptide. Previous studies have suggested that aside from providing energy, metabolism influences oxidative stress resistance different organisms. To explore this potential role mechanism, we characterized wild-type putA mutant strains Escherichia coli . Initial assays revealed strain was significantly more sensitive than parental strain. Expression PutA restored resistance, confirming depletion responsible for phenotype. Treatment cells with increased hydroperoxidase I (encoded katG ) expression activity. Furthermore, failed respond proline, indicating critical mechanism protection. global regulator OxyR activates along several other genes involved defense. In addition , grxA (glutaredoxin 1) trxC (thioredoxin 2) regulon, implicating Proline shown generate hydrogen peroxide, increases tolerance E. via preadaptive effect involving endogenous peroxide production enhanced catalase-peroxidase
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