Cloning of new Rhodococcus extradiol dioxygenase genes and study of their distribution in different Rhodococcus strains.
Four extradiol dioxygenase genes which encode enzymes active against catechol and substituted catechols were cloned from two different Rhodococcus strains, and their nucleotide sequences were determined. A catechol 2,3-dioxygenase gene (edoC) was shown to be identical to the previously described ipbC gene from the isopropylbenzene operon of Rhodococcus erythropolis. Amino acid sequences deduced from the three other genes (edoA, edoB and edoD) were shown to have various degrees of homology to different extradiol dioxygenases. The EdoA and EdoB dioxygenases were classified as belonging to the third family of type I oxygenases and represented two new subfamilies, whereas the EdoD dioxygenase was a type II enzyme. Analysis of six Rhodococcus strains revealed a wide distribution of the above dioxygenase genes. Rhodococcus sp. 11 was shown to harbour all four of the analysed dioxygenase genes. Nucleotide sequences homologous to the edoB gene were present in all of the strains, including R. erythropolis NCIMB 13065, which did not utilize any of the aromatic compounds analysed. The latter finding points to the existence of a silent pathway(s) for degradation of aromatic compounds in this Rhodococcus strain.
Kulakov
Leonid A
LA
1 The Questor Centre, David Keir Building, The Queen's University of Belfast, Belfast BT9 5AG, UK and School of Biology and Biochemistry, Medical Biology Centre, The Queen's University of Belfast, Belfast BT9 7BL, UK.
Delcroix
Valerie A
VA
1 The Questor Centre, David Keir Building, The Queen's University of Belfast, Belfast BT9 5AG, UK and School of Biology and Biochemistry, Medical Biology Centre, The Queen's University of Belfast, Belfast BT9 7BL, UK.
Larkin
Michael J
MJ
1 The Questor Centre, David Keir Building, The Queen's University of Belfast, Belfast BT9 5AG, UK and School of Biology and Biochemistry, Medical Biology Centre, The Queen's University of Belfast, Belfast BT9 7BL, UK.
Ksenzenko
Vladimir N
VN
2 Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Science, Pushchino, Moscow region, Russia.
Kulakova
Anna N
AN
1 The Questor Centre, David Keir Building, The Queen's University of Belfast, Belfast BT9 5AG, UK and School of Biology and Biochemistry, Medical Biology Centre, The Queen's University of Belfast, Belfast BT9 7BL, UK.
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics*; D001483:Base Sequence; D050557:Catechol 2,3-Dioxygenase; D049308:Dioxygenases; D005798:Genes, Bacterial / Q000235:genetics*; D008969:Molecular Sequence Data; D010105:Oxygenases / Q000235:genetics*; D016133:Polymerase Chain Reaction; D012240:Rhodococcus / Q000201:enzymology* / Q000235:genetics; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA
D001426:Bacterial Proteins; D010105:Oxygenases; D049308:Dioxygenases; D050557:Catechol 2,3-Dioxygenase