Uniformity of the genes of bacterial dehalogenases acting on fluoroacetate.

Two genes encoding haloacetate dehalogenases, H-1 and H-2, are closely linked on a plasmid from Moraxellu sp. strain B. H-1 predominantly acts on fluoroacetate, but H-2 does not. To elucidate the molecular relationship between the two enzymes, we compared their structural genes. Two restriction fragments of the plasmid DNA were subcloned on M13 phages and their nucleotide sequences were determined. The sequence of each fragment contained an open reading frame that was identified as the structural gene for each of the two dehalogenases on the basis of the following criteria; N-terminal amino acid sequence, amino acid composition, and molecular mass. The genes for H-1 and H-2, designated &hHl and khH2, respectively, had Merent sizes (885 bp and 675 bp) and G + C contents (58.3% and 53.4%). Sequence analysis revealed no homology between the two genes. We concluded that the dehalogenases H-1 and H-2 have no enzyme-evolutionary relationship. The deduced amino acid sequence of the &hHl gene showed significant similarity to those of three hydrolases of Pseudomonasputida and a haloalkane dehalogenase of Xanthobacter rurtotrophicus. The &hH2 coding region was sandwiched between two repeated sequences about 1.8 kb long, which might play a part in the frequent spontaneous deletion of &hH2 from the plasmid.

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Lack of homology between two haloacetate dehalogenase genes encoded on a plasmid from Moraxella sp. strain B

Kawasaki

Tsuda

Matsushita

et al. 1992

Journal of General Microbiology

107

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Uniformity of the genes of bacterial dehalogenases acting on fluoroacetate.

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Lack of homology between two haloacetate dehalogenase genes encoded on a plasmid from Moraxella sp. strain B

Lack of homology between two haloacetate dehalogenase genes encoded on a plasmid from Moraxella sp. strain B

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