Abstract
In methanotrophic bacteria, methane is oxidized to methanol by the enzyme methane monooxygenase (MMO). The soluble MMO enzyme complex from Methylocystis sp. strain M also oxidizes a wide range of aliphatic and aromatic compounds, including trichloroethylene. In this study, heterologous DNA probes from the type II methanotroph Methylosinus trichosporium OB3b were used to isolate souble MMO (sMMO) genes from the type II methanotroph Methylocystis sp. strain M. sMMO genes from strain M are clustered on the chromosome and show a high degree of identity with the corresponding genes from Methylosinus trichosporium OB3b. Sequencing and phylogenetic analysis of the 16S rRNA gene from Methylocystis sp. strain M have confirmed that it is most closely related to the type II methanotroph Methylocystis parvus OBBP, which, unlike Methylocystis sp. strain M, does not possess an sMMO. A similar phylogenetic analysis using the pmoA gene, which encodes the 27-kDa polypeptide of the particulate MMO, also places Methylocystis sp. strain M firmly in the genus Methylocystis. This is the first report of isolation and characterization of methane oxidation genes from methanotrophs of the genus Methylocystis.
Full Text
The Full Text of this article is available as a PDF (401.2 KB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Bowman J. P., Sly L. I., Stackebrandt E. The phylogenetic position of the family Methylococcaceae. Int J Syst Bacteriol. 1995 Jan;45(1):182–185. doi: 10.1099/00207713-45-1-182. [DOI] [PubMed] [Google Scholar]
- Brusseau G. A., Bulygina E. S., Hanson R. S. Phylogenetic analysis and development of probes for differentiating methylotrophic bacteria. Appl Environ Microbiol. 1994 Feb;60(2):626–636. doi: 10.1128/aem.60.2.626-636.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cardy D. L., Laidler V., Salmond G. P., Murrell J. C. Molecular analysis of the methane monooxygenase (MMO) gene cluster of Methylosinus trichosporium OB3b. Mol Microbiol. 1991 Feb;5(2):335–342. doi: 10.1111/j.1365-2958.1991.tb02114.x. [DOI] [PubMed] [Google Scholar]
- Cardy D. L., Laidler V., Salmond G. P., Murrell J. C. The methane monooxygenase gene cluster of Methylosinus trichosporium: cloning and sequencing of the mmoC gene. Arch Microbiol. 1991;156(6):477–483. doi: 10.1007/BF00245395. [DOI] [PubMed] [Google Scholar]
- Colby J., Dalton H. Resolution of the methane mono-oxygenase of Methylococcus capsulatus (Bath) into three components. Purification and properties of component C, a flavoprotein. Biochem J. 1978 May 1;171(2):461–468. doi: 10.1042/bj1710461. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Felsenstein J. Phylogenies from molecular sequences: inference and reliability. Annu Rev Genet. 1988;22:521–565. doi: 10.1146/annurev.ge.22.120188.002513. [DOI] [PubMed] [Google Scholar]
- Green J., Dalton H. Protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath). A novel regulatory protein of enzyme activity. J Biol Chem. 1985 Dec 15;260(29):15795–15801. [PubMed] [Google Scholar]
- Gutell R. R., Larsen N., Woese C. R. Lessons from an evolving rRNA: 16S and 23S rRNA structures from a comparative perspective. Microbiol Rev. 1994 Mar;58(1):10–26. doi: 10.1128/mr.58.1.10-26.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hanson R. S., Hanson T. E. Methanotrophic bacteria. Microbiol Rev. 1996 Jun;60(2):439–471. doi: 10.1128/mr.60.2.439-471.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Holmes A. J., Costello A., Lidstrom M. E., Murrell J. C. Evidence that particulate methane monooxygenase and ammonia monooxygenase may be evolutionarily related. FEMS Microbiol Lett. 1995 Oct 15;132(3):203–208. doi: 10.1016/0378-1097(95)00311-r. [DOI] [PubMed] [Google Scholar]
- Holmes A. J., Owens N. J., Murrell J. C. Detection of novel marine methanotrophs using phylogenetic and functional gene probes after methane enrichment. Microbiology. 1995 Aug;141(Pt 8):1947–1955. doi: 10.1099/13500872-141-8-1947. [DOI] [PubMed] [Google Scholar]
- Koh S. C., Bowman J. P., Sayler G. S. Soluble Methane Monooxygenase Production and Trichloroethylene Degradation by a Type I Methanotroph, Methylomonas methanica 68-1. Appl Environ Microbiol. 1993 Apr;59(4):960–967. doi: 10.1128/aem.59.4.960-967.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lipscomb J. D. Biochemistry of the soluble methane monooxygenase. Annu Rev Microbiol. 1994;48:371–399. doi: 10.1146/annurev.mi.48.100194.002103. [DOI] [PubMed] [Google Scholar]
- Maidak B. L., Larsen N., McCaughey M. J., Overbeek R., Olsen G. J., Fogel K., Blandy J., Woese C. R. The Ribosomal Database Project. Nucleic Acids Res. 1994 Sep;22(17):3485–3487. doi: 10.1093/nar/22.17.3485. [DOI] [PMC free article] [PubMed] [Google Scholar]
- McDonald I. R., Kenna E. M., Murrell J. C. Detection of methanotrophic bacteria in environmental samples with the PCR. Appl Environ Microbiol. 1995 Jan;61(1):116–121. doi: 10.1128/aem.61.1.116-121.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Murrell J. C. Molecular genetics of methane oxidation. Biodegradation. 1994 Dec;5(3-4):145–159. doi: 10.1007/BF00696456. [DOI] [PubMed] [Google Scholar]
- Neefs J. M., Van de Peer Y., De Rijk P., Goris A., De Wachter R. Compilation of small ribosomal subunit RNA sequences. Nucleic Acids Res. 1991 Apr 25;19 (Suppl):1987–2015. doi: 10.1093/nar/19.suppl.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nguyen H. H., Shiemke A. K., Jacobs S. J., Hales B. J., Lidstrom M. E., Chan S. I. The nature of the copper ions in the membranes containing the particulate methane monooxygenase from Methylococcus capsulatus (Bath). J Biol Chem. 1994 May 27;269(21):14995–15005. [PubMed] [Google Scholar]
- Nielsen A. K., Gerdes K., Degn H., Murrell J. C. Regulation of bacterial methane oxidation: transcription of the soluble methane mono-oxygenase operon of Methylococcus capsulatus (Bath) is repressed by copper ions. Microbiology. 1996 May;142(Pt 5):1289–1296. doi: 10.1099/13500872-142-5-1289. [DOI] [PubMed] [Google Scholar]
- Nordlund P., Dalton H., Eklund H. The active site structure of methane monooxygenase is closely related to the binuclear iron center of ribonucleotide reductase. FEBS Lett. 1992 Aug 3;307(3):257–262. doi: 10.1016/0014-5793(92)80690-i. [DOI] [PubMed] [Google Scholar]
- Oldenhuis R., Vink R. L., Janssen D. B., Witholt B. Degradation of chlorinated aliphatic hydrocarbons by Methylosinus trichosporium OB3b expressing soluble methane monooxygenase. Appl Environ Microbiol. 1989 Nov;55(11):2819–2826. doi: 10.1128/aem.55.11.2819-2826.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rosenzweig A. C., Frederick C. A., Lippard S. J., Nordlund P. Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane. Nature. 1993 Dec 9;366(6455):537–543. doi: 10.1038/366537a0. [DOI] [PubMed] [Google Scholar]
- Saunders S. E., Burke J. F. Rapid isolation of miniprep DNA for double strand sequencing. Nucleic Acids Res. 1990 Aug 25;18(16):4948–4948. doi: 10.1093/nar/18.16.4948. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Semrau J. D., Chistoserdov A., Lebron J., Costello A., Davagnino J., Kenna E., Holmes A. J., Finch R., Murrell J. C., Lidstrom M. E. Particulate methane monooxygenase genes in methanotrophs. J Bacteriol. 1995 Jun;177(11):3071–3079. doi: 10.1128/jb.177.11.3071-3079.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Shingler V. Signal sensing by sigma 54-dependent regulators: derepression as a control mechanism. Mol Microbiol. 1996 Feb;19(3):409–416. doi: 10.1046/j.1365-2958.1996.388920.x. [DOI] [PubMed] [Google Scholar]
- Smith D. D., Dalton H. Solubilisation of methane monooxygenase from Methylococcus capsulatus (Bath). Eur J Biochem. 1989 Jul 1;182(3):667–671. doi: 10.1111/j.1432-1033.1989.tb14877.x. [DOI] [PubMed] [Google Scholar]
- Stainthorpe A. C., Lees V., Salmond G. P., Dalton H., Murrell J. C. The methane monooxygenase gene cluster of Methylococcus capsulatus (Bath). Gene. 1990 Jul 2;91(1):27–34. doi: 10.1016/0378-1119(90)90158-n. [DOI] [PubMed] [Google Scholar]
- Stainthorpe A. C., Murrell J. C., Salmond G. P., Dalton H., Lees V. Molecular analysis of methane monooxygenase from Methylococcus capsulatus (Bath). Arch Microbiol. 1989;152(2):154–159. doi: 10.1007/BF00456094. [DOI] [PubMed] [Google Scholar]
- Stirling D. I., Dalton H. Properties of the methane mono-oxygenase from extracts of Methylosinus trichosporium OB3b and evidence for its similarity to the enzyme from Methylococcus capsulatus (Bath). Eur J Biochem. 1979 May 2;96(1):205–212. doi: 10.1111/j.1432-1033.1979.tb13030.x. [DOI] [PubMed] [Google Scholar]
- Tsien H. C., Hanson R. S. Soluble methane monooxygenase component B gene probe for identification of methanotrophs that rapidly degrade trichloroethylene. Appl Environ Microbiol. 1992 Mar;58(3):953–960. doi: 10.1128/aem.58.3.953-960.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Uchiyama H., Nakajima T., Yagi O., Nakahara T. Role of heterotrophic bacteria in complete mineralization of trichloroethylene by Methylocystis sp. strain M. Appl Environ Microbiol. 1992 Sep;58(9):3067–3071. doi: 10.1128/aem.58.9.3067-3071.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Woodland M. P., Dalton H. Purification and characterization of component A of the methane monooxygenase from Methylococcus capsulatus (Bath). J Biol Chem. 1984 Jan 10;259(1):53–59. [PubMed] [Google Scholar]
- Zahn J. A., DiSpirito A. A. Membrane-associated methane monooxygenase from Methylococcus capsulatus (Bath). J Bacteriol. 1996 Feb;178(4):1018–1029. doi: 10.1128/jb.178.4.1018-1029.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]