Genome sequence of n-alkane-degrading Hydrocarboniphaga effusa strain AP103T (ATCC BAA-332T).

Hydrocarboniphaga effusa strain AP103(T) (ATCC BAA-332(T)) is a member of the Gammaproteobacteria utilizing n-alkanes as the sole source of carbon and energy. Here we report the draft genome sequence of AP103(T), which consists of 5,193,926 bp with a G + C content of 65.18%.

Involvement of two transport systems and a specific porin in the uptake of phthalate by Burkholderia spp.

Burkholderia spp. that degrade phthalate have an ABC transporter-type phthalate transport system (OphFGH) and a specific porin (OphP) in addition to a permease-type phthalate transporter (OphD). OphFGH has a lower K(m) and higher V(max) than OphD, which affects how the bacteria grow.

Examination and expansion of the substrate range of m-hydroxybenzoate hydroxylase.

The gene encoding m-hydroxybenzoate hydroxylase (mobA) was cloned from Comamonas testosteroni GZ39. MobA converts m-hydroxybenzoate and to a lesser extent p-hydroxybenzoate to protocatechuate. To explore the structural and functional relationships in phenolic acid monooxygenases, MobA was subjected to in vitro mutagenesis by error-prone PCR and the mutant MobAs were screened for their ability to oxidize phenol or 3-aminophenol.

Hydrocarboniphaga effusa gen. nov., sp. nov., a novel member of the gamma-Proteobacteria active in alkane and aromatic hydrocarbon degradation.

Novel alkane-degrading strains of bacteria were isolated from soil contaminated with fuel oil from a leaking underground tank in New Jersey, USA. Two phenotypically similar strains (designated AP102 and AP103T) possessed 16S rRNA sequences unique among the majority of known hydrocarbon-degrading bacteria. The 16S rRNA sequences showed a moderate but distant relationship to the genus Nevskia and a substantial similarity to strains that had previously been isolated for growth on phenol (in Japan) and on toluene (in Canada) by other researchers.

Characterization and regulation of the genes for a novel anthranilate 1,2-dioxygenase from Burkholderia cepacia DBO1.

Anthranilate (2-aminobenzoate) is an important intermediate in tryptophan metabolism. In order to investigate the degradation of tryptophan through anthranilate by Burkholderia cepacia, several plasposon mutations were constructed of strain DBO1 and one mutant with the plasposon insertion in the anthranilate dioxygenase (AntDO) genes was chosen for further study. The gene sequence obtained from flanking DNA of the plasposon insertion site revealed unexpected information.