4-Methylphthalate catabolism in Burkholderia (Pseudomonas) cepacia Pc701 : a gene encoding a phthalate-specific permease forms part of a novel gene cluster

作者: C. P. Saint , P. Romas

DOI: 10.1099/00221287-142-9-2407

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摘要: We have determined the entire nucleotide sequence of a 4.4 kbp fragment pMOP, plasmid involved in 4-methylphthalate catabolism Burkholderia cepacia (formerly Pseudomonas cepacia) Pc701. Two complete ORFs were identified and termed mopA mopB. mopB encodes permease which is member superfamily symport proteins found both prokaryotes eukaryotes. Functionality was assigned to MopB by detailed analysis predicted amino acid sequence, resulting identification 12 hydrophobic membrane-spanning domains motifs associated with this class protein. An assay developed demonstrate function substrate uptake. Of 4-methylphthalate, 4-hydroxyisophthalate, benzoate, p-toluate phthalate, only uptake phthalate demonstrated, suggesting that two carboxyl groups ortho position are essential for recognition. The protein MopA showed significant levels homology reductase implicated aromatic aliphatic catabolism, contained recognized as binding ADP flavin moieties FAD/NAD. Northern hybridization experiments cotranscribed, but expression seen cells grown on not closely related structural analogues, including phthalate. may be situated at 3′-terminus cistron about 10 size. isolation characterization gene lead other permeases bacterial biodegradation processes possibly construction strains enhanced degradative abilities.

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