Cloning and nucleotide sequence of the 2,3-dihydroxybiphenyl dioxygenase gene from the PCB-degrading strain of Pseudomonas paucimobilis Q1
- 1 May 1988
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 27 (11), 3990-3996
- https://doi.org/10.1021/bi00411a015
Abstract
The bphC gene encoding 2,3-dihydroxybiphenyl dioxygenase was cloned from biphenyl-degrading and chlorinated biphenyl-degrading Pseudomonas paucimobilis Q1, and its complete nucleotide sequence was determined. The DNA-derived protein sequence provides the primary structure of 298 amino acids. Polyclonal antibodies raised aganist this protein from P. paucimobilis Q1 failed to cross-react with the previously isolated 2,3-dihydroxybiphenyl dioxygenase from Pseudomonas pseudoalcaligenes KF707 [Furukawa, K., and Arimura, N. (1987) J. Bacteriol. 169, 924-927. Furukawa, K., Arimura, N., and Miyazaki T. (1987) J. Bacteriol. 169, 427-429], despite the close similarities of these proteins in terms of their native as well as subunit molecular weights, cofactor, and enzymatic activities. The sequence homology of the 2,3-dihydroxybiphenyl dioxygenase from the two different sources in examined.This publication has 4 references indexed in Scilit:
- Cloning of a gene cluster encoding biphenyl and chlorobiphenyl degradation in Pseudomonas pseudoalcaligenesJournal of Bacteriology, 1986
- Deoxyribonucleic acid sequence of a gene from the Pseudomonas transposon TN501 encoding mercuric reductaseBiochemistry, 1983
- Generation of protein-reactive antibodies by short peptides is an event of high frequency: implications for the structural basis of immune recognition.Proceedings of the National Academy of Sciences, 1983
- A procedure for the isolation of deoxyribonucleic acid from micro-organismsJournal of Molecular Biology, 1961