Glycerol metabolism of Lactobacillus rhamnosus ATCC 7469: Cloning and expression of two glycerol kinase genes

Journal of Molecular Microbiology and Biotechnology

Volumn 7, Issue 4, 2004, Pages 170-181

  Alvarez, María De Fátima ^a   Medina, Roxana ^a,b   Pasteris, Sergio E ^b   Strasser De Saad, Ana M ^a,b   Sesma, Fernando ^a  

^a CENTRO DE REFERENCIA PARA LACTOBACILOS CERELA CONICET   (Argentina)

^b UNIVERSIDAD NACIONAL DE TUCUMÁN   (Argentina)

Author keywords

Diacetyl; Glycerol kinase; Glycerol metabolism; Lactobacillus rhamnosus

Indexed keywords

GLYCEROL; GLYCEROL 3 PHOSPHATE DEHYDROGENASE; GLYCEROL KINASE;

ARTICLE; BACTERIAL GENE; BACTERIAL METABOLISM; BACTERIAL STRAIN; CULTURE MEDIUM; DNA SEQUENCE; ENZYME ACTIVITY; GENE EXPRESSION; GENE SEQUENCE; GENETIC ANALYSIS; LACTOBACILLUS RHAMNOSUS; MICROBIAL GENETICS; MOLECULAR CLONING; MOLECULAR INTERACTION; NONHUMAN; NUCLEOTIDE SEQUENCE;

ACETATES; ADAPTATION, PHYSIOLOGICAL; AEROBIOSIS; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BASE SEQUENCE; CLONING, MOLECULAR; CONSERVED SEQUENCE; DIACETYL; DNA, BACTERIAL; GENE EXPRESSION REGULATION, BACTERIAL; GENES, BACTERIAL; GLUCOSE; GLYCEROL; GLYCEROL KINASE; GLYCEROLPHOSPHATE DEHYDROGENASE; LACTIC ACID; LACTOBACILLUS; MOLECULAR SEQUENCE DATA; OPERON; PROMOTER REGIONS (GENETICS); RNA, BACTERIAL; RNA, MESSENGER; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, DNA;

LACTOBACILLUS; LACTOBACILLUS RHAMNOSUS;

EID: 4644281537     PISSN: 14641801     EISSN: None     Source Type: Journal    
DOI: 10.1159/000079826     Document Type: Article

References (45)

1. Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A., and Struhl, K. Short Protocols in Molecular Biology, Fourth Edition. John Wiley and Sons Inc., New York, 1999.
2. Bolotin, A., Wincker, P., Mauger, S., Jaillon, O., Malarme, K., Weissenbach, J., Ehrlich, S.D., and Sorokin, A. The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403. Genome Res. 2001,11:731-753.
3. Branny, P., de la Torre, F., and Garel, J.R. An operon encoding three glycolytic enzymes in Lactobacillus delbrueckii subsp. bulgaricus: Glyceraldehyde 3-phosphate dehydrogenase, phosphoglycerate kinase and triosephosphate isomerase. Microbiology 1998, 144:905-914.
4. Cancilla, M.R., Hillier, A.J., and Davidson, B.E. Lactococcus lactis glyceraldehyde 3-phosphate dehydrogenase gene, gap: Further evidence for strongly biased codon usage in glycolytic pathway genes. Microbiology 1995, 141:1027-1036.
5. Charrier, V., Buckley, E., Parsonage, D., Galinier, A., Darbon, E., Jaquinod, M., Forest, E., Deutscher, J., and Claiborne, A. Cloning and sequencing of two enterococcal glpK genes and regulation of the encoded glycerol kinases by phosphoenolpyruvate-dependent, phosphotransferase system-catalyzed phosphorylation of a single histidyl residue. J. Biol. Chem. 1997,272:14166-14174.
6. Chen, X., and Wu, R. Direct amplification of unknown genes and fragments by uneven polymerase chain reaction. Gene 1997, 185:195-199.
7. Claisse, O., and Lonvaud-Funel, A. Assimilation of glycerol by a strain of Lactobacillus collinoides isolated from cider. Food Microbiol. 2000, 17:513-519.
8. Cocaign-Bousquet, M., Garrigues, C., Loubiere, P., and Lindley, N.D. Physiology of pyruvate metabolism in Lactococcus lactis. Antonie Van Leeuwenhoek 1996, 70:253-267.
9. Collins, M.D., Phillips, B.A., and Zanoni, P. Deoxyribonucleic acid homology studies of Lactobacillus casei, Lactobacillus paracasei sp. nov., subsp. paracasei and subsp. tolerans, and Lactobacillus rhamnosus sp. nov., comb. nov. Int. J. Syst. Bacteriol. 1989, 39:105-108.
10. Condon, S. Responses of lactic acid bacteria to oxigen. FEMS Microbiol. Rev. 1987, 46:269-280.
11. Daniel, R., Bobik, T.A., and Gottschalk, G. Biochemistry of coenzyme B12-dependent glycerol and diol dehydratases and organization of the encoding genes. FEMS Microbiol. Rev. 1998,22:553-566.
12. Darbon, E., Ito, K., Huang, H.S., Yoshimoto, T., Poncet, S., and Deutscher, J. Glycerol transport and phosphoenolpyruvate-dependent enzyme I and HPr-catalysed phosphorylation of glycerol kinase in Thermus flavus. Microbiology 1999, 145:3205-3212.
13. Darbon, E., Servant, P., Poncet, S., and Deutscher, J. Antitermination by GlpP, catabolite repression via CcpA and inducer exclusion triggered by P-GlpK dephosphorylation control Bacillus subtilis glpFK expression. Mol. Microbiol. 2002, 43:1039-1052.
14. Deutscher, J., Bauer, B., and Sauerwald, H. Regulation of glycerol metabolism in Enterococcus faecalis by phosphoenolpyruvate-dependent phosphorylation of glycerol kinase catalyzed by enzyme I and HPr of the phosphotransferase system. J. Bacteriol. 1993, 175:3730-3733.
15. Dovat, A.M., Reinbold, G.W., Hammond, E.G., and Vedamuthu, E.R. Lipolytic and proteolytic activity of enterococci and lactic group streptococci isolated from young cheddar cheese. J. Milk Food Tech. 1970, 33:365-372.
16. Drinan, D.F., Robin, S., and Cogan, T.M. Citric acid metabolism in hetero- and homofermentative lactic acid bacteria. Appl. Environ. Microbiol. 1976, 31:481-486.
17. Feese, M., Pettigrew, D.W., Meadow, N.D., Roseman, S., and Remington, S.J. Cation-promoted association of a regulatory and target protein is controlled by protein phosphorylation. Proc. Natl. Acad. Sci. USA 1994, 91:3544-3548.
18. Flaherty, K.M., McKay, D.B., Kabsch, W., and Holmes, K.C. Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein. Proc. Natl. Acad. Sci. USA 1991, 88:5041-5045.
19. Fortnagel, P. Glycolysis. In Sonenshein, A.L., Hoch, J.A., and Losick, R. (eds.). Bacillus subtilis and Other Gram-Positive Bacteria. Biochemistry, Physiology and Molecular Genetics. Washington D.C., ASM PRESS, 1996, pp. 171-180.
20. Hill, E.C., Wenzel, F.W., and Barreto, A. Colorimetric method for detection of microbiological spoilage in citrus juice. Food Tech. 1954, 8:168-171.
21. Holmberg, C., Beijer, L., Rutberg, B., and Rutberg, L. Glycerol catabolism in Bacillus subtilis: Nucleotide sequence of the genes encoding glycerol kinase (glpK) and glycerol 3-phosphate dehydrogenase (glpD). J. Gen. Microbiol. 1990,136:2367-2375.
22. Holmberg, C., and Rutberg, B. Cloning of the glycerol kinase gene of Bacillus subtilis. FEMS Microbiol. Lett. 1989, 49:151-155.
23. Hugenholtz, J. Citrate metabolism in lactic acid bacteria. FEMS Microbiol. Rev. 1993, 12:165-178.
24. Hugenholtz, J., and Kleerebezem, M. Metabolic engineering of lactic acid bacteria: Overview of the approaches and results of pathway rerouting involved in food fermentations. Curr. Opin. Biotechnol. 1999, 10:492-497.
25. Hugenholtz, J., Kleerebezem, M., Starrenburg, M., Delcour, J., de Vos, W., and Hols, P. Lactococcus lactis as a cell factory for high-level diacetyl production. Appl. Environ. Microbiol. 2000,66:4112-4114.
26. Kleerebezem, M., Boekhorst, J., van Kranenburg, R. et al. Complete genome sequence of Lactobacillus plantarum WCFS1. Proc. Natl. Acad. Sci. USA 2003, 100:1990-1995.
27. Lin, E.C.C. Dissimilatory pathways for sugars, polyols, and carboxylates. In Neidhardt, F.C., Curtiss, R. 3rd, Ingraham, J.L, Lin, E.C.C., Low, K.B., Maganasik, B., Reznikoff, W.S., Riley, M., Schaechter, M., and Umbarger, H.E. (eds.). Escherichia coli and Salmonella: Cellular and Molecular Biology. Washington D.C., ASM PRESS, 1996, vol. 2, pp. 307-342.
28. Lonvaud-Funel, A. Recherches sur les bactéries lactiques du vin. Fonctions métaboliques, croissance, génétique plasmidique. 1986, Thèse Université de Bordeaux II (France).
29. Lowry, O.H., Rosebrough, W.J., Farr, A.L., and Randall, R.J. Protein measurements with the folin phenol reagent. J. Biol. Chem. 1951, 193:265-275.
30. Medina de Figueroa, R., Alvarez, F., de Ruiz Holgado, A.P., Oliver, F., and Sesma, F. Citrate utilization by homo- and heterofermentative lactobacilli. Microbiol. Res. 2000, 154:313-320.
31. Medina de Figueroa, R.M., Benito de Cardenas, I.L., Sesma, F., Alvarez, F., de Ruiz Holgado, A.P., and Oliver, G. Inducible transport of citrate in Lactobacillus rhamnosus ATCC 7469. J. Appl. Bacteriol. 1996, 81:348-354.
32. Parsonage, D., Luba, J., Mallett, T.C., and Claiborne, A. The soluble alpha-glycerophosphate oxidase from Enterococcus casseliflavus. Sequence homology with the membrane-associated dehydrogenase and kinetic analysis of the recombinant enzyme. J. Biol. Chem. 1998,273:23812-23822.
33. Pasteris, S.E., and Strasser de Saad, A.M. Characterization of glycerol kinase and NAD-independent glycerol 3-phosphate dehydrogenase from Pediococcus pentosaceus N5p. Lett. Appl. Microbiol. 1998, 27:93-97.
34. Pettigrew, D.W., Liu, W.Z., Holmes, C., Meadow, N.D., and Roseman, S. A single amino acid change in Escherichia coli glycerol kinase abolishes glucose control of glycerol utilization in vivo. J. Bacteriol. 1996, 178:2846-2852.
35. Pettigrew, D.W., Ma, D.P., Conrad, C.A., and Johnson, J.R. Escherichia coli glycerol kinase. Cloning and sequencing of the glpK gene and the primary structure of the enzyme. J. Biol. Chem. 1988, 263:135-139.
36. Pospiech, A., and Neumann, B. A versatile quickprep of genomic DNA from gram-positive bacteria. Trends Genet. 1995, 11:217-218.
37. Raibaud, P., Caulet, M., Galpin, J., and Mocquot, G. Studies in bacterial flora of the alimentary tract of pigs. II. Streptococci: Selective enumeration and differentiation of dominant group. J. Appl. Bacteriol. 1961, 24:285-291.
38. Rao, D.R., and Reddy, J.C. Effects of lactic acid fermentation of milk on milk lipids. J. Food Sci. 1984, 49:748-750.
39. Sauvageot, N., Muller, C., Hartke A., Auffray Y., and Laplace J.M. Characterisation of the diol dehydratase pdu operon of Lactobacillus collinoides. FEMS Microbiol. Lett. 2002, 209:66-71.
40. Schutz, H., and Radler, F. Anaerobic reduction of glycerol to propanediol-1,3 by Lactobacillus brevis and Lactobacillus reuteri. Syst. Appl. Microbiol. 1984, 5:169-178.
41. Schweizer, H.P., Jump, R., and Po, C. Structure and gene-polypeptide relationships of the region encoding glycerol diffusion facilitator (glpF) and glycerol kinase (glpK) of Pseudomonas aeruginosa. Microbiology 1997, 143:1287-1297.
42. Talarico, T.L., and Dobrogosz, W.J. Chemical characterization of an antimicrobial substance produced by Lactobacillus reuteri. Antimicrob. Agents Chemother. 1989, 33:674-679.
43. Veiga da Cunha, M., and Foster, M.A. Sugar-glycerol cofermentations in lactobacilli: The fate of lactate. J. Bacteriol. 1992, 174:1013-1019.
44. Weickert, M.J., and Chambliss, G.H. Site-directed mutagenesis of a catabolite repression operator sequence in Bacillus subtilis. Proc. Natl. Acad. Sci. USA 1990, 87:6238-6242.
45. White, A.G.C., Krampitz, L.O., and Werkman CH. Methods for the direct determination of diacetyl in tissue and bacterial filtrates. Arch. Biochem. 1946, 9:229-234.