Identification of large linear plasmids in Arthrobacter spp. encoding the degradation of quinaldine to anthranilate.
Arthrobacter nitroguajacolicus Rü61a, which utilizes quinaldine as sole source of carbon and energy, was shown to contain a conjugative linear plasmid of approximately 110 kb, named pAL1. It exhibits similarities with other linear plasmids from Actinomycetales in that it has proteins covalently attached to its 5' ends. Southern hybridization with probes for the genes encoding quinaldine 4-oxidase and N-acetylanthranilate amidase indicated that pAL1 contains the gene cluster encoding the degradation of quinaldine to anthranilate. A mutant of strain Rü61a that had lost pAL1 indeed could not convert quinaldine, but was still able to grow on anthranilate. Conjugative transfer of pAL1 to the plasmid-less mutant of strain Rü61a and to Arthrobacter nicotinovorans DSM 420 (pAO1) occurred at frequencies of 5.4x10(-4) and 2.0x10(-4) per recipient, respectively, and conferred the ability to utilize quinaldine. Five other quinaldine-degrading Gram-positive strains were isolated from soil samples; 16S rDNA sequence analysis suggested the closest relationship to different Arthrobacter species. Except for strain K2-29, all isolates contained a pAL1-like linear plasmid carrying genes encoding quinaldine conversion. A 478 bp fragment that on pAL1 represents an intergenic region showed 100 % sequence identity in all isolates harbouring a pAL1-like plasmid, suggesting horizontal dissemination of the linear plasmid among the genus Arthrobacter.
Overhage
Jörg
J
Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität Münster, Corrensstraße 3, D-48149 Münster, Germany.
Sielker
Sonja
S
Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität Münster, Corrensstraße 3, D-48149 Münster, Germany.
Homburg
Stefan
S
Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität Münster, Corrensstraße 3, D-48149 Münster, Germany.
Parschat
Katja
K
Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität Münster, Corrensstraße 3, D-48149 Münster, Germany.
Fetzner
Susanne
S
Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität Münster, Corrensstraße 3, D-48149 Münster, Germany.
D000581:Amidohydrolases / Q000235:genetics / Q000378:metabolism; D001173:Arthrobacter / Q000145:classification / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D001673:Biodegradation, Environmental; D003227:Conjugation, Genetic; D016521:Electrophoresis, Gel, Pulsed-Field; D008667:Metalloproteins / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000235:genetics / Q000378:metabolism; D010957:Plasmids / Q000235:genetics*; D011798:Quinaldines / Q000737:chemistry / Q000378:metabolism*; D017422:Sequence Analysis, DNA; D062367:ortho-Aminobenzoates / Q000737:chemistry / Q000378:metabolism*
D008667:Metalloproteins; D011798:Quinaldines; D062367:ortho-Aminobenzoates; C031385:anthranilic acid; C067844:N-acetylanthranilic acid; C037073:2-methylquinoline; D010088:Oxidoreductases; C080754:quinaldine oxidoreductase; D000581:Amidohydrolases; C019665:amidase