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Journal of Bacteriology, May 2007, p. 3855-3867, Vol. 189, No. 10
0021-9193/07/$08.00+0     doi:10.1128/JB.00089-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Complete Nucleotide Sequence of the 113-Kilobase Linear Catabolic Plasmid pAL1 of Arthrobacter nitroguajacolicus Rü61a and Transcriptional Analysis of Genes Involved in Quinaldine Degradation ^,

Katja Parschat,¹ Jörg Overhage,^1, Axel W. Strittmatter,² Anke Henne,^2, Gerhard Gottschalk,² and Susanne Fetzner^1*

Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität Münster, D-48149 Münster, Germany,¹ Laboratorium für Genomanalyse, Institut für Mikrobiologie und Genetik, Georg-August-Universität Göttingen, D-37077 Göttingen, Germany²

Received 17 January 2007/ Accepted 27 February 2007

The nucleotide sequence of the linear catabolic plasmid pAL1 from the 2-methylquinoline (quinaldine)-degrading strain Arthrobacter nitroguajacolicus Rü61a comprises 112,992 bp. A total of 103 open reading frames (ORFs) were identified on pAL1, 49 of which had no annotatable function. The ORFs were assigned to the following functional groups: (i) catabolism of quinaldine and anthranilate, (ii) conjugation, and (iii) plasmid maintenance and DNA replication and repair. The genes for conversion of quinaldine to anthranilate are organized in two operons that include ORFs presumed to code for proteins involved in assembly of the quinaldine-4-oxidase holoenzyme, namely, a MobA-like putative molybdopterin cytosine dinucleotide synthase and an XdhC-like protein that could be required for insertion of the molybdenum cofactor. Genes possibly coding for enzymes involved in anthranilate degradation via 2-aminobenzoyl coenzyme A form another operon. These operons were expressed when cells were grown on quinaldine or on aromatic compounds downstream in the catabolic pathway. Single-stranded 3' overhangs of putative replication intermediates of pAL1 were predicted to form elaborate secondary structures due to palindromic and superpalindromic terminal sequences; however, the two telomeres appear to form different structures. Sequence analysis of ORFs 101 to 103 suggested that pAL1 codes for one or two putative terminal proteins, presumed to be covalently bound to the 5' termini, and a multidomain telomere-associated protein (Tap) comprising 1,707 amino acids. Even if the putative proteins encoded by ORFs 101 to 103 share motifs with the Tap and terminal proteins involved in telomere patching of Streptomyces linear replicons, their overall sequences and domain structures differ significantly.

Published ahead of print on 2 March 2007.

Supplemental material for this article may be found at http://jb.asm.org/.

Present address: Centre for Microbial Diseases and Immunity Research, University of British Columbia, 2259 Lower Mall, Vancouver, BC, V6T 1Z4, Canada.

Present address: Qiagen GmbH, Qiagen Strasse 1, 40724 Hilden, Germany.