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Journal of Bacteriology, April 2006, p. 2586-2592, Vol. 188, No. 7
0021-9193/06/$08.00+0     doi:10.1128/JB.188.7.2586-2592.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Product Repression of Alkane Monooxygenase Expression in Pseudomonas butanovora

D. M. Doughty,1 L. A. Sayavedra-Soto,2 D. J. Arp,2 and P. J. Bottomley1,3*

Department of Microbiology,1 Department of Botany and Plant Pathology,2 Department of Crop and Soil Science, Oregon State University, Corvallis, Oregon3

Received 6 December 2005/ Accepted 23 January 2006

Physiological and regulatory mechanisms that allow the alkane-oxidizing bacterium Pseudomonas butanovora to consume C2 to C8 alkane substrates via butane monooxygenase (BMO) were examined. Striking differences were observed in response to even- versus odd-chain-length alkanes. Propionate, the downstream product of propane oxidation and of the oxidation of other odd-chain-length alkanes following ß-oxidation, was a potent repressor of BMO expression. The transcriptional activity of the BMO promoter was reduced with as little as 10 µM propionate, even in the presence of appropriate inducers. Propionate accumulated stoichiometrically when 1-propanol and propionaldehyde were added to butane- and ethane-grown cells, indicating that propionate catabolism was inactive during growth on even-chain-length alkanes. In contrast, propionate consumption was induced (about 80 nmol propionate consumed · min–1 · mg protein–1) following growth on the odd-chain-length alkanes, propane and pentane. The induction of propionate consumption could be brought on by the addition of propionate or pentanoate to the growth medium. In a reporter strain of P. butanovora in which the BMO promoter controls ß-galactosidase expression, only even-chain-length alcohols (C2 to C8) induced ß-galactosidase following growth on acetate or butyrate. In contrast, both even- and odd-chain-length alcohols (C3 to C7) were able to induce ß-galactosidase following the induction of propionate consumption by propionate or pentanoate.

* Corresponding author. Mailing address: Department of Microbiology, Nash Hall, Room 220, Oregon State University, Corvallis, OR 97331-3804. Phone: (541) 737-4441. Fax: (541) 737-0496. E-mail: Peter.Bottomley{at}orst.edu.

Journal of Bacteriology, April 2006, p. 2586-2592, Vol. 188, No. 7
0021-9193/06/$08.00+0     doi:10.1128/JB.188.7.2586-2592.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Doughty, D. M., Kurth, E. G., Sayavedra-Soto, L. A., Arp, D. J., Bottomley, P. J. (2008). Evidence for Involvement of Copper Ions and Redox State in Regulation of Butane Monooxygenase in Pseudomonas butanovora. J. Bacteriol. 190: 2933-2938 [Abstract] [Full Text]  
  • Kurth, E. G., Doughty, D. M., Bottomley, P. J., Arp, D. J., Sayavedra-Soto, L. A. (2008). Involvement of BmoR and BmoG in n-alkane metabolism in 'Pseudomonas butanovora'. Microbiology 154: 139-147 [Abstract] [Full Text]  
  • Doughty, D. M., Halsey, K. H., Vieville, C. J., Sayavedra-Soto, L. A., Arp, D. J., Bottomley, P. J. (2007). Propionate inactivation of butane monooxygenase activity in 'Pseudomonas butanovora': biochemical and physiological implications. Microbiology 153: 3722-3729 [Abstract] [Full Text]  
  • Dubbels, B. L., Sayavedra-Soto, L. A., Arp, D. J. (2007). Butane monooxygenase of 'Pseudomonas butanovora': purification and biochemical characterization of a terminal-alkane hydroxylating diiron monooxygenase. Microbiology 153: 1808-1816 [Abstract] [Full Text]  
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