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CRP Regulates D-Lactate Oxidation in Shewanella oneidensis MR-1

MR-1 is a heterotrophic facultative anaerobe that respires using various organic and inorganic compounds. This organism has served as a model to study bacterial metabolic and regulatory systems that facilitate their survival in redox-stratified environments. The expression of many anaerobic respirat...

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Bibliographic Details
Published in:Frontiers in microbiology 2017-05, Vol.8, p.869-869
Main Authors: Kasai, Takuya, Kouzuma, Atsushi, Watanabe, Kazuya
Format: Article
Language:English
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Summary:MR-1 is a heterotrophic facultative anaerobe that respires using various organic and inorganic compounds. This organism has served as a model to study bacterial metabolic and regulatory systems that facilitate their survival in redox-stratified environments. The expression of many anaerobic respiratory genes in MR-1, including those for the reduction of fumarate, dimethyl sulfoxide, and metal oxides, is regulated by cyclic AMP receptor protein (CRP). However, relatively little is known about how this organism regulates the expression of catabolic enzymes catalyzing the oxidation of organic compounds, including lactate. Here, we investigated transcriptional mechanisms for the (SO_1522) and (SO_1521) genes, which encode putative lactate permease and D-lactate dehydrogenase, respectively, and demonstrate that CRP regulates their expression in MR-1. We found that a -deletion mutant of MR-1 (Δ ) showed impaired growth on D-lactate. Complementary expression of in Δ restored the ability to grow on D-lactate, indicating that the deficient growth of Δ on D-lactate is attributable to decreased expression of . transcription and electrophoretic mobility shift assays reveal that CRP positively regulates the expression of the and genes by directly binding to an upstream region of . Taken together, these results indicate that CRP is a global transcriptional regulator that coordinately regulates the expression of catabolic and respiratory pathways in MR-1, including D-lactate dehydrogenase and anaerobic terminal reductases.
ISSN:1664-302X
1664-302X
DOI:10.3389/fmicb.2017.00869