Synthesis of glycine betaine from exogenous choline in the moderately halophilic bacterium Halomonas elongata

Applied and Environmental Microbiology

Volumn 64, Issue 10, 1998, Pages 4095-4097

  Cánovas, David ^a,b   Vargas, Carmen ^a   Csonka, Laszlo N ^b   Ventosa, Antonio ^a   Nieto, Joaquín J ^a  

^a UNIVERSITY OF SEVILLE   (Spain)

^b PURDUE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BETAINE; CHOLINE; SODIUM CHLORIDE;

AMINE TRANSPORT; ARTICLE; BACTERIAL GROWTH; BACTERIAL METABOLISM; BIOACCUMULATION; BIOTRANSFORMATION; CULTURE MEDIUM; GENE EXPRESSION REGULATION; HALOPHILIC BACTERIUM; MICHAELIS CONSTANT; NONHUMAN; OSMOTIC STRESS; OXIDATION;

BACTERIA (MICROORGANISMS); HALOMONAS ELONGATA; NEGIBACTERIA;

EID: 0345647089     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.64.10.4095-4097.1998     Document Type: Article

References (18)

1. Boch, J., B. Kempf, and E. Bremer. 1994. Osmoregulation in Bacillus subtilis: synthesis of the osmoprotectant glycine betaine from exogenously provided choline. J. Bacteriol. 176:5364-5371.
2. Boch, J., B. Kempf, R. Schmid, and E. Bremer. 1996. Synthesis of the osmoprotectant glycine betaine in Bacillus subtilis: characterization of gbsAB genes. J. Bacteriol. 178:5121-5129.
3. Cánovas, D., C. Vargas, E. Bremer, A. Ventosa, and J. J. Nieto. Unpublished data.
4. Cánovas, D., C. Vargas, L. N. Csonka, A. Ventosa, and J. J. Nieto. 1996. Osmoprotectants in Halomonas elongata: high-affinity betaine transport system and choline-betaine pathway. J. Bacteriol. 178:7221-7226.
5. Cánovas, D., C. Vargas, F. Iglesias-Guerra, L. N. Csonka, D. Rhodes, A. Ventosa, and J. J. Nieto. 1997. Isolation and characterization of salt-sensitive mutants of the moderate halophile Halomonas elongata and cloning of the ectoine synthesis genes. J. Biol. Chem. 272:25794-25801.
6. Cohen, G. N., and R. H. Rickenberg. 1956. Concentration specifique reversible des aminoi acides chez E. coli. Ann. Inst. Pasteur Paris 91:693-720.
7. Eshoo, M. W. 1988. lac fusion analysis of the bet genes of Escherichia coli: regulation by osmolarity, temperature, oxygen, choline, and glycine betaine. J. Bacteriol. 170:5208-5215.
8. Galinski, E. A. 1995. Osmoadaptation in bacteria. Adv. Microb. Physiol. 1995:273-328.
9. Kushner, D. J. 1978. Life in high salt and solute concentrations: halophilic bacteria, p. 317-368. In D. J. Kushner (ed.), Microbial life in extreme environments. Academic Press, London, United Kingdom.
10. Lamark, T., T. P. Røkenes, J. McDougall, and A. R. Strøm. 1996. The complex bet promoters of Escherichia coli: regulation by oxygen (ArcA), choline (BetI), and osmotic stress. J. Bacteriol. 178:1655-1662.
11. Landfald, B., and A. R. Strøm. 1986. Choline-glycine betaine pathway confers a high level of osmotic tolerance in Escherichia coli. J. Bacteriol. 165: 849-855.
12. McCue, K. F., and A. D. Hanson. 1992. Salt-inducible betaine aldehyde dehydrogenase from sugar beet: cDNA cloning and expression. Plant Mol. Biol. 18:1-11.
13. Ventosa, A., and J. J. Nieto. 1995. Biotechnological applications and potentialities of halophilic microorganisms. World J. Microbiol. Biotechnol. 11: 85-94.
14. Ventosa, A., J. J. Nieto, and A. Oren. 1998. The biology of moderately halophilic aerobic bacteria. Microbiol. Mol. Biol. Rev. 62:504-544.
15. Vijaranakul, U., M. J. Nadakavukaren, D. O. Bayles, B. J. Wilkinson, and R. K. Jayaswal. 1997. Characterization of a NaCl-sensitive Staphylococcus aureus mutant and rescue of the NaCl-sensitive phenotype by glycine betaine but not by other compatible solutes. Appl. Environ. Microbiol. 63:1889-1897.
16. Vreeland, R. H., C. D. Litchfield, E. L. Martin, and E. Elliot. 1980. Halomonas elongata, a new genus and species of extremely salt-tolerant bacteria. Int. J. Syst. Bacteriol. 30:485-495.
17. Weigel, P., C. Lerma, and A. D. Hanson. 1988. Choline oxidation by intact spinach chloroplasts. Plant Physiol. 86:54-60.
18. Weretilnyk, E. A., and A. D. Hanson. 1990. Molecular cloning of a plant betaine-aldehyde dehydrogenase, an enzyme implicated in adaptation to salinity and drought. Proc. Natl. Acad. Sci. USA 87:2745-2749.