Genes for the synthesis of the osmoprotectant glycine betaine from choline in the moderately halophilic bacterium Halomonas elongata DSM 3043, USA.
The genes involved in the oxidative pathway of choline to glycine betaine in the moderate halophile Halomonas elongata DSM 3043 were isolated by functional complementation of an Escherichia coli strain defective in glycine betaine synthesis. The cloned region was able to mediate the oxidation of choline to glycine betaine in E. coli, but not the transport of choline, indicating that the gene(s) involved in choline transport are not clustered with the glycine betaine synthesis genes. Nucleotide sequence analysis of a 4.6 kb segment from the cloned DNA revealed the occurrence of three ORFs (betIBA) apparently arranged in an operon. The deduced betI gene product exhibited features typical for DNA-binding regulatory proteins. The deduced BetB and BetA proteins showed significant similarity to soluble glycine betaine aldehyde dehydrogenases and membrane-bound choline dehydrogenases, respectively, from a variety of organisms. Evidence is presented that BetA is able to oxidize both choline and glycine betaine aldehyde and therefore can mediate both steps in the synthesis of glycine betaine.
Cánovas
David
D
Laboratory for Microbiology, Department of Biology, Philipps University, MarburgD-35032, Marburg, Germany2.|Department of Microbiology and Parasitology, Faculty of Pharmacy, University of Seville, 41012 Seville, Spain1.
Vargas
Carmen
C
Department of Microbiology and Parasitology, Faculty of Pharmacy, University of Seville, 41012 Seville, Spain1.
Kneip
Susanne
S
Laboratory for Microbiology, Department of Biology, Philipps University, MarburgD-35032, Marburg, Germany2.
Morón
Marı A-Jesús
MA
Department of Microbiology and Parasitology, Faculty of Pharmacy, University of Seville, 41012 Seville, Spain1.
Ventosa
Antonio
A
Department of Microbiology and Parasitology, Faculty of Pharmacy, University of Seville, 41012 Seville, Spain1.
Bremer
Erhard
E
Laboratory for Microbiology, Department of Biology, Philipps University, MarburgD-35032, Marburg, Germany2.
Nieto
Joaquı N J
JNJ
Department of Microbiology and Parasitology, Faculty of Pharmacy, University of Seville, 41012 Seville, Spain1.
D000429:Alcohol Oxidoreductases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D000445:Aldehyde Oxidoreductases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D001622:Betaine / Q000378:metabolism*; D050728:Betaine-Aldehyde Dehydrogenase; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D002794:Choline / Q000378:metabolism*; D050545:Choline Dehydrogenase; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D005798:Genes, Bacterial; D020632:Halomonas / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D009876:Operon / Q000235:genetics; D014882:Water-Electrolyte Balance / Q000235:genetics*
D001426:Bacterial Proteins; C119698:BetL protein, Listeria monocytogenes; D002352:Carrier Proteins; D001622:Betaine; D000429:Alcohol Oxidoreductases; D050545:Choline Dehydrogenase; D000445:Aldehyde Oxidoreductases; D050728:Betaine-Aldehyde Dehydrogenase; D002794:Choline