Reconstitution of the trimethylamine oxide reductase regulatory elements of Shewanella oneidensis in Escherichia coli

Several bacteria can grow by using small organic compounds such as trimethylamine oxide (TMAO) as electron acceptors. In Shewanella species, the TMAO reductase respiratory system is encoded by the torECAD operon. We showed that production of the TMAO reductase of S. oneidensis was induced by TMAO an...

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Bibliographic Details
Published in:Journal of bacteriology Vol. 184; no. 5; p. 1262
Main Authors: Gon, Stéphanie, Patte, Jean-Claude, Dos Santos, Jean-Philippe, Méjean, Vincent
Format: Journal Article
Language:English
Published: United States 01.03.2002
Subjects:
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Base Sequence
Enzyme Induction
Escherichia coli Proteins
Gene Expression Regulation, Bacterial
Methylamines - metabolism
Methylamines - pharmacology
Molecular Sequence Data
Multigene Family
Operon
Oxidoreductases, N-Demethylating - biosynthesis
Oxidoreductases, N-Demethylating - genetics
Oxygen - pharmacology
Periplasmic Proteins
Phosphorylation
Phosphotransferases
Promoter Regions, Genetic - genetics
Shewanella - enzymology
Shewanella - genetics
Shewanella - growth & development
Signal Transduction
Transcription Factors - genetics
Transcription Factors - metabolism
ISSN:0021-9193
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Summary:Several bacteria can grow by using small organic compounds such as trimethylamine oxide (TMAO) as electron acceptors. In Shewanella species, the TMAO reductase respiratory system is encoded by the torECAD operon. We showed that production of the TMAO reductase of S. oneidensis was induced by TMAO and repressed by oxygen, and we noticed that a three-gene cluster (torSTR) encoding a complex two-component regulatory system was present downstream of the torECAD operon. We introduced the torSTR gene cluster into Escherichia coli and showed that this regulatory gene cluster is involved in TMAO induction of the torE promoter but plays no role in the oxygen control. The TorR response regulator was purified, and gel shift and footprinting experiments revealed that TorR binds to a single region located about 70 bases upstream of the transcription start site of the tor structural operon. By deletion analysis, we confirmed that the TorR operator site is required for induction of the tor structural promoter. As the TMAO regulatory system of S. oneidensis is homologous to that of E. coli, we investigated a possible complementation between the TMAO regulatory components of the two bacteria. Interestingly, TorS(ec), the TMAO sensor of E. coli, was able to transphosphorylate TorR(so), the TMAO response regulator of S. oneidensis.
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ISSN:0021-9193
DOI:10.1128/JB.184.5.1262-1269.2002