Cloning, sequencing, and expression of isopropylbenzene degradation genes from Psuedomonas sp. strain JR1: identification of isopropylbenzene dioxygenase that mediates trichloroethene oxidation

Article Abstract:

The genes encoding enzymes involved in the catabolism of isopropylbenzene (IPB) in Psuedomonas sp. strain JR1 have been identified in a cosmid clone consisting of seven open reading frames. The ipbA gene codes for IPB dioxygenase, ipbB codes for 2,3-dihydro-2,3-dihydroxy-IPB dehydrogenase and ipbC codes for 3-isopropylcatechol 2,3-dioxygenase. The amino acid sequence of the clone is similar to that of the proteins involved in biphenyl-degradation in gram-positive and gram-negative bacteria. IPB is the inducer substrate for trichloroethene oxidation in Pseudomonas.

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Studies on the isopropylbenzene 2,3-dioxygenase and the 3-isopropylcatechol 2,3-dioxygenase genes encoded by the linear plasmid of Rhodcoccus erythropolis BD2

Article Abstract:

The isopropylbenzene (IPB) catabolic genes of Rhodococcus erythropolis were cloned and sequenced to determine the molecular and biochemical basis of IPB oxidation and trichloroethene (TCE) co-oxidation. Synthesis of IPB ferredoxin, IPB reductase and terminal dioxygenase is encoded by IPB catabolic gene cluster, ipbA1A2A3A4C. Furthermore, the five clustered genes are homologous to the corresponding proteins that function in the degradative pathways of Escherichia coli.

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Construction and use of an ipb DNA module to generate Pseudomonas strains with constitutive trichloroethene and isopropylbenzene oxidation activity

Article Abstract:

Pseudomonas strains with the ability to degrade isopropylbenzene (IPB) and tricholoroethane (TCE) are developed using an ipb DNA module. Results from the localization of transcriptional start points of the ipbA genes indicate that ipb gene expressions are regulated in response to IPB at the transcriptional level. The mutant Pseudomonas sp. strain JR1 exhibited the ability to efficiently degrade TCE after the induction of TCE-oxidizing oxygenase.

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