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Journal of Bacteriology, January 2004, p. 22-28, Vol. 186, No. 1
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.1.22-28.2004

Multiple Formate Dehydrogenase Enzymes in the Facultative Methylotroph Methylobacterium extorquens AM1 Are Dispensable for Growth on Methanol

Ludmila Chistoserdova,1 Markus Laukel,2,3 Jean-Charles Portais,4 Julia A. Vorholt,2 and Mary E. Lidstrom1,5*

Department of Chemical Engineering,1 Department of Microbiology, University of Washington, Seattle, Washington 98195-2180,5 Laboratoire des Interactions Plantes Micro-organismes, INRA/CNRS, 31326 Castanet-Tolosan, France,2 Max-Planck-Institut für Terrestrische Mikrobiologie, 35043 Marburg, Germany,3 INSA Toulouse, Complexe Scientifique de Rangueil, 31077 Toulouse, France4

Received 12 August 2003/ Accepted 2 October 2003

Formate dehydrogenase has traditionally been assumed to play an essential role in energy generation during growth on C1 compounds. However, this assumption has not yet been experimentally tested in methylotrophic bacteria. In this study, a whole-genome analysis approach was used to identify three different formate dehydrogenase systems in the facultative methylotroph Methylobacterium extorquens AM1 whose expression is affected by either molybdenum or tungsten. A complete set of single, double, and triple mutants was generated, and their phenotypes were analyzed. The growth phenotypes of the mutants suggest that any one of the three formate dehydrogenases is sufficient to sustain growth of M. extorquens AM1 on formate, while surprisingly, none is required for growth on methanol or methylamine. Nuclear magnetic resonance analysis of the fate of [13C]methanol revealed that while cells of wild-type M. extorquens AM1 as well as cells of all the single and the double mutants continuously produced [13C]bicarbonate and 13CO2, cells of the triple mutant accumulated [13C]formate instead. Further studies of the triple mutant showed that formate was not produced quantitatively and was consumed later in growth. These results demonstrated that all three formate dehydrogenase systems must be inactivated in order to disrupt the formate-oxidizing capacity of the organism but that an alternative formate-consuming capacity exists in the triple mutant.

* Corresponding author. Mailing address: Department of Chemical Engineering, University of Washington, Box 352180, Seattle, WA 98195-2180. Phone: (206) 616-5282. Fax: (206) 616-5721. E-mail: lidstrom{at}u.washington.edu.

Journal of Bacteriology, January 2004, p. 22-28, Vol. 186, No. 1
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.1.22-28.2004




This article has been cited by other articles:

  • Crowther, G. J., Kosaly, G., Lidstrom, M. E. (2008). Formate as the Main Branch Point for Methylotrophic Metabolism in Methylobacterium extorquens AM1. J. Bacteriol. 190: 5057-5062 [Abstract] [Full Text]  
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