Analysis of two formaldehyde oxidation pathways in Methylobacillus flagellatus KT, a ribulose monophosphate cycle methylotroph

Microbiology

Volumn 146, Issue 1, 2000, Pages 233-238

  Chistoserdova, Ludmila ^a   Gomelsky, Larissa ^d,e   Vorholt, Julia A ^a,c   Gomelsky, Mark ^d,e   Tsygankov, Yuri D ^d   Lidstrom, Mary E ^a,b  

^a University of Washington   (United States)

^b UNIVERSITY OF WASHINGTON   (United States)

^c Max Plank Inst Terrestrische M   (Germany)

^d Institute of Genetics   (Russian Federation)

^e UNIVERSITY OF WYOMING   (United States)

Author keywords

Formaldehyde oxidation; Methylotroph; Ribulose monophosphate cycle; Tetrahydromethanopterin

Indexed keywords

FORMALDEHYDE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; METHENYLTETRAHYDROFOLATE CYCLOHYDROLASE; PHOSPHOGLUCONATE DEHYDROGENASE; RIBULOSE PHOSPHATE;

ARTICLE; BACTERIAL METABOLISM; CONTROLLED STUDY; GENE MUTATION; GENE SEQUENCE; METHYLOBACILLUS FLAGELLATUS; METHYLOBACTERIUM; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; OXIDATION; PRIORITY JOURNAL;

BACTERIA (MICROORGANISMS); METHYLOBACILLUS; METHYLOBACILLUS FLAGELLATUS; METHYLOBACILLUS FLAGELLATUS KT; METHYLOBACTERIUM; METHYLOBACTERIUM EXTORQUENS; PROKARYOTA;

EID: 0033978320     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-146-1-233     Document Type: Article

References (23)

1. Anthony, C. (1982). The Biochemistry of Methylotropbs. London: Academic Press.
2. Barber, R. D. & Donohue, T. J. (1998). Function of a glutathione-dependent formaldehyde dehydrogenase in Rhodobacter sphaeroides formaldehyde oxidation and assimilation. Biochemistry 37, 330-337.
3. Chistoserdov, A. Y., Chistoserdova, L. V., McIntire, W. S. & Lidstrom, M. E. (1994). Genetic organization of the man gene cluster in Methylobacterium extorquens AM1: complete nucleotide sequence and generation and characteristics of man mutants. J Bacteriol 176, 4052-4065.
4. Chistoserdova, L. V., Chistoserdov, A. Y., Schklyar, N. L., Baev, M. V. & Tsygankov, Y. D. (1991). Oxidative and assimilative enzyme activities in continuous cultures of the obligate methylotroph Methylobacillus flagellatum. Antonie Leeuwenboek 60, 101-107.
5. 1 transfer enzymes and coenzymes linking methylotrophic bacteria and methanogenic archaea. Science 281, 99-102.
6. Ditta, G., Schmidhauser, T., Yakobson, F., Lu, P., Liang, X., Finlay, D., Guiney, D. & Helinski, D. (1985). Plasmids related to the broad host range vector, pRK290, useful for gene cloning and monitoring gene expression. Plasmid 13, 149-153.
7. Gak, E. R., Tsygankov, Y. D. & Chistoserdov, A. Y. (1997). Organization of methylamine utilization genes (mau) in 'Methylobacillus flagellatum' KT and analysis of mau mutants. Microbiology 143, 1827-1835.
8. Harder, W., Attwood, M. & Quayle, J. R. (1973). Methanol assimilation by Hyphomicrobium spp. J Gen Microbiol 78, 115-163.
9. 1 Compounds, pp. 126-132. Edited by M. E. Lidstrom & F. R. Tabita. Dordrecht: Kluwer.
10. Kiriuchin, M. Y., Kletsova, L. V., Chistoserdov, A. Y. & Tsygankov, Y. D. (1988). Properties of glucose 6-phosphate and 6-phosphogluconate dehydrogenases of the obligate methylotroph Methylobacillus flagellatum KT. FEMS Microbiol Lett 52, 199-204.
11. Kletsova, L. V., Govorukhina, N. I., Tsygankov, Y. D. & Trosenko, Y. A. (1987). Metabolism of the obligate methylotroph Methylobacillus flagellatum. Mikrobiologiya 56, 901-906.
12. Kletsova, L. V., Chibisova, E. S. & Tsygankov, Y. D. (1988). Mutants of the obligate methylotroph Methylobacillus flagellatum KT defective in genes of the ribulose monophosphate cycle of formaldehyde fixation. Arch Microbiol 149, 441-446.
13. Kletsova, L. V., Kiriukhin, M. Y., Chistoserdov, A. Y. & Tsygankov, Y. D. (1990). Glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from Methylobacillus flagellatum. Methods Enzymol 188, 335-339.
14. Maniatis, T., Fritsch, E. F. & Sambrook, J. (1982). Molecular Cloning: a Laboratory Manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
15. Meinkoth, J. & Wahl, G. (1984). Hybridization of nucleic acids immobilized on solid supports. Anal Biochem 138, 267-284.
16. Pomper, B. K., Vorholt, J. A., Chistoserdova, L., Lidstrom, M. E. & Thauer, R. K. (1999). A methenyl tetrahydromethanopterin cyclohydrolase and a methenyl tetrahydrofolate cyclohydrolase in Methylobacterium extorquens AM1. Eur J Biochem 261, 475-480.
17. Saito, H. & Miura, K.-I. (1963). Preparation of transforming deoxyribonucleic acid by phenol treatment. Biochim Biophys Acta 72, 619-629.
18. Simon, R., Priefer, U. & Puhler, A. (1983). Vector plasmids for in vivo manipulations of Gram-negative bacteria. In Molecular Genetics of the Bacteria-Plant Interaction, pp. 98-106. Edited by A. Puhler. Berlin: Springer.
19. Tsygankov, Y. D., Kazakova, S. M. & Serebrijski, I. G. (1990). Genetic mapping of the obligate methylotroph Methylobacillus flagellatum KT: characteristics of prime plasmids and mapping of the chromosome in time-of-enrry units. J Bacteriol 172, 2747-2754.
20. Van Gijsegem, F. & Toussaint, A. (1982). Chromosome transfer and R-prime formation by an RP4::mini-Mu derivative in Escherichia coli, Salmonella typhimurium, Klebsiella pneumoniae, and Proteus mirabilis. Plasmid 7, 30-44.
21. Vinopal, R. T., Hillman, J. D., Schulman, H., Reznikoff, W. S. & Fraenkel, D. G. (1975). New phosphogluconate isomerase mutants of Escherichia coli. J Bacteriol 122, 1172-1174.
22. Vorholt J. A., Chistoserdova, L., Stolyar, S. M., Lidstrom, M. E. & Thauer, R. K. (1999). Distribution of tetrahydromethanopterin-dependent enzymes in methylotrophic bacteria and phylogeny of methenyl tetrahydromethanopterin cydohydrolases. J Bacteriol 181, 5750-5757.
23. Whitaker, J. R. & Granum, P. E. (1980). An absolute method for protein determination based on difference in absorbance at 235 and 280 nm. Anal Biochem 109, 156-159.