Amphitrite ornata, a marine worm, contains two dehaloperoxidase genes

Amphitrite ornata, a terebellid polychaete, inhabits marine environments that are contaminated by biogenically produced halometabolites. These halogenated organic compounds are toxic and quite diverse. To survive in this environment, A. ornata produces a novel dehaloperoxidase (DHP I) that detoxifie...

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Bibliographic Details
Published in:Marine biotechnology (New York, N.Y.) N.Y.), 2001-05, Vol.3 (3), p.287-292
Main Authors: Han, K, Woodin, S A, Lincoln, D E, Fielman, K T, Ely, B
Format: Article
Language:English
Subjects:
Alleles
Amino acid sequences
Amino acids
Amphitrite ornata
Complementary DNA
Dehaloperoxidase
Deoxyribonucleic acid
dhpA gene
dhpB gene
DNA
DNA libraries
Gene polymorphism
Gene sequencing
Genes
Marine
Marine environment
Marine invertebrates
Marine pollution
Nucleotide sequence
Organic compounds
PCR
Polymerase chain reaction
Polymorphism
Restriction fragment length polymorphism
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Summary:Amphitrite ornata, a terebellid polychaete, inhabits marine environments that are contaminated by biogenically produced halometabolites. These halogenated organic compounds are toxic and quite diverse. To survive in this environment, A. ornata produces a novel dehaloperoxidase (DHP I) that detoxifies haloaromatic compounds. In this study we identified and characterized two dehaloperoxidase genes, designated dhpA and dhpB, from an A. ornata complementary DNA library. The deduced amino acid sequences (DHP A and DHP B) of the two dhp genes both contain 137 amino acid residues, but they differ at 5 amino acid positions. Allelic variation was observed for both genes as well. Polymerase chain reaction-restriction fragment length polymorphism assays of genomic DNA from 19 in individuals showed that each individual contains both the dhpA and the dhpB genes. Therefore, the two types of DHP are encoded by separate genes and are not alleles of a single gene. Furthermore, DHP A and DHP B may have different substrate specificities since they have amino acid differences in the active site.
ISSN:1436-2228
1436-2236
DOI:10.1007/s10126-001-0003-8