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Genetics and Molecular Biology |
Department of Microbiology and Parasitology, Faculty of Pharmacy, University of Seville, 41012 Seville, Spain1
Laboratory for Microbiology, Department of Biology, Philipps University, MarburgD-35032, Marburg, Germany2
Author for correspondence: Joaquín J. Nieto. Tel: +34 95 4556765. Fax: +34 954 628162. e-mail: jjnieto{at}cica.es
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.
Keywords: moderate halophiles, Halomonas elongata, bet genes, osmoregulation, compatible solutes
Abbreviations: BADH, glycine betaine aldehyde dehydrogenase; CDH, choline dehydrogenase
The EMBL accession number for the sequence reported in this paper is AJ238780.
a Present address: Departamento de Biotecnología Microbiana, Centro Nacional de Biotecnología, CSIC, Cantoblanco, 28049 Madrid, Spain.
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