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Journal of Bacteriology, January 2003, p. 142-147, Vol. 185, No. 1
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.1.142-147.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Growth of Mycobacteria on Carbon Monoxide and Methanol

Sae W. Park,1 Eun H. Hwang,1 Hyuck Park,1 Jeong A. Kim,1 Jinho Heo,1 Key H. Lee,1 Taeksun Song,1,{dagger} Eungbin Kim,1 Young T. Ro,2 Si W. Kim,3 and Young M. Kim1*

Department of Biology, Yonsei University, Seoul 120-749,1 Laboratory of Biochemistry, Konkuk College of Medicine, Chungju 380-701,2 Department of Environmental Engineering, Chosun University, Kwangju 501-759, Korea3

Received 8 August 2002/ Accepted 8 October 2002

Several mycobacterial strains, such as Mycobacterium flavescens, Mycobacterium gastri, Mycobacterium neoaurum, Mycobacterium parafortuitum, Mycobacterium peregrinum, Mycobacterium phlei, Mycobacterium smegmatis, Mycobacterium tuberculosis, and Mycobacterium vaccae, were found to grow on carbon monoxide (CO) as the sole source of carbon and energy. These bacteria, except for M. tuberculosis, also utilized methanol as the sole carbon and energy source. A CO dehydrogenase (CO-DH) assay, staining by activity of CO-DH, and Western blot analysis using an antibody raised against CO-DH of Mycobacterium sp. strain JC1 (formerly Acinetobacter sp. strain JC1 [J. W. Cho, H. S. Yim, and Y. M. Kim, Kor. J. Microbiol. 23:1-8, 1985]) revealed that CO-DH is present in extracts of the bacteria prepared from cells grown on CO. Ribulose bisphosphate carboxylase/oxygenase (RubisCO) activity was also detected in extracts prepared from all cells, except M. tuberculosis, grown on CO. The mycobacteria grown on methanol, except for M. gastri, which showed hexulose phosphate synthase activity, did not exhibit activities of classic methanol dehydrogenase, hydroxypyruvate reductase, or hexulose phosphate synthase but exhibited N,N-dimethyl-4-nitrosoaniline-dependent methanol dehydrogenase and RuBisCO activities. Cells grown on methanol were also found to have dihydroxyacetone synthase. Double immunodiffusion revealed that the antigenic sites of CO-DHs, RuBisCOs, and dihydroxyacetone synthases in all mycobacteria tested are identical with those of the Mycobacterium sp. strain JC1 enzymes.

* Corresponding author. Mailing address: Molecular Microbiology Laboratory, Department of Biology, Yonsei University, Seoul 120-749, Korea. Phone: 82-2-2123-2658. Fax: 82-2-312-5657. E-mail: young547{at}yonsei.ac.kr.

{dagger} Present address: The Genome Research Center for Respiratory Pathogens, Yonsei University College of Medicine, Seoul 12-752, Korea.

Journal of Bacteriology, January 2003, p. 142-147, Vol. 185, No. 1
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.1.142-147.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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