Abstract
The 165-kb megaplsmid pAO1 of Arthrobacter nicotinovorans enables its host to grow on nicotine as carbon, nitrogen and energy source. The plasmid has a modular structure with DNA segments flanked by mobile genetic elements. The presence of gene modules specific for l-nicotine, d-nicotine and γ-N-methylami-nobutyrate catabolism, for the biosyntheses of the molybdenum cofactor required by the molybdenum enzymes of the pathway, for the two subunits of a small multi-drug resistance pump and for gene products for the protection from oxidative stress generated by oxidation of nicotine blue, underscores the notion that this plasmid evolved specifically to fulfil the task of nicotine degradation.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Andreesen JR, Fetzner S (2002) The molybdenum-containing hydroxylases of nicotinate, isonicotinate, and nicotine. Metal Ions Biol Sys 39:405–430
Armstrong DW, Wang X, Lee J-T, Liu Y-S (1999) Enantiomeric composition of nornicotine, anatabine, and anabasine in tobacco. Chiriality 11:82–84
Baitsch D, Sandu C, Brandsch R, Igloi GL (2001) Gene cluster on pAO1 of Arthrobacter nicotinovorans involved in degradation of the plant alkaloid nicotine: cloning, purification, and characterization of 2,6-dihydroxypyridine 3-hydroxylase. J Bacteriol 183:5262–5267
Brandsch R (2006) Microbiology and biochemistry of nicotine degradation. Appl Microbiol Biotechnol 69:493–498
Brandsch R, Bichler V (1991) Autoflavinylation of apo-6-hydroxy-d-nicotine oxidase. J Biol Chem 266:19056–19062
Chiribau C-B, Sandu C, Fraaije M, Schiltz E, Brandsch R (2004) A novel γ-N-methylaminobutyrate demethylating oxidase involved in catabolism of the tobacco alkaloid nicotine by Arthrobacter nicotinovorans pAO1. Eur J Biochem 271:4677–4684
Chiribau C-B, Sandu C, Igloi GL, Brandsch R (2005) Characterization of PmfR, the transcriptional activator of the pAO1-borne purU-mabO-folD operon of Arthrobacter nicotinovorans J Bacteriol 187:3062–3070
Chiribau C-B, Mihasan M, Ganas P, Igloi GL, Artenie V, Brandsch R (2006) Final steps in the catabolism of nicotine. Deamination versus demethylation of γ-N-methylaminobutyrate. FEBS J 273:1528–1536
Fuhrmann S, Ferner M, Jeffke T, Henne A, Gottschalk G, Meyer O (2003) Complete nucleotide sequence of the circular megaplsmid pHCG3 of Oligotropha carboxidovorans : function in the chemolithoautotrophic utilization of CO, H2 and CO2. Gene 322:67–75
Ganas P, Mihasan M, Igloi GL, Brandsch R (2007) A two-component small multidrug resistance pump functions as a metabolic valve during nicotine catabolism by Arthrobacter nicotinovorans. Microbiol 153:1546–1555
Gloger M, Decker K (1969) Zum Mechanismus der Induktion nicotinabbauender Enzyme in Arthrobacter oxydans. Z Naturforsch 24b:1016–1025
Igloi GL, Brandsch R (2003) Sequence of the 165-kilobase catabolic plasmid pAO1 from Arthrobacter nicotinovorans and identification of a pAO1-dependent nicotine uptake system. J Bacteriol 185:1976–1989
Jones D, Keddie RM (1992) The genus Arthrobacter. In: Balows A, Truper AHG, Dwarkin M, Harder W, Schleifer KH (ed) The Prokaryotes, vol. 2. Springer, Heidelberg, pp 1283–1299
Kodama Y, Yamamoto H, Amano N, Amchi T (1992) Reclassification of two species of Arthrobacter oxydans and proposal of Arthrobacter nicotinovorans sp nov. Int J Syst Bacteriol 42:234–239
Knackmuss H-J, Beckmann W (1973) The structure of nicotine blue from Arthrobacter oxidans Arch Mikrobiol 90:167–169
Koetter JWA, Schulz G (2005) Crystal structure of 6-hydroxy-d -nicotine oxidase from Arthrobacter nicotinovorans. J Mol Biol 352:418–428
Menéndez C, Igloi GL, Brandsch R (1997) IS 1473, a putative insertion sequence identified in the plasmid pAO1 from Arthrobacter nicotinovorans : isolation, characterization and distribution among Arthrobacter species. Plasmid 37:35–41
Mihasan M, Chiribau C-B, Friedrich T, Artenie V, Brandsch R (2007) An NAD(P)H-nicotine blue oxidoreductase is part of the nicotine regulon and may protect Arthrobacter nicotinovorans from oxidative stress during nicotine catabolism. Appl Environ Microbiol 73:2479–2485
Mongodin EF, Shapir N, Daugherty SC, DeBoy RT, Emerson JB, Shvartzbeyn A, Radune D, Vamathevan J, Riggs F, Grinberg V, Khouri H, Wackett LP, Nelson KE, Sadowsky MJ (2006) Secrets of soil survival revealed by the genome sequence of Arthrobacter aurescens TC1. PLoS Genet 2:2094–2106
Neumann M, Schulte M, Jünemann N, Stöcklein W, Leimkühler S (2006),Rhodobacter capsulatus XdhC is involved in molybdenum cofactor binding and insertion into xanthine dehydrogenase. J Biol Chem 281:15701–15708
Parschat K, Overhage J, Strittmatter AW, Henne A, Gottschalk G, Fetzner S (2007) Complete nucleotide sequence of the 113-kilobase linear catabolic plasmid pAL1 of Arthrobacter nitroguajacolicus Rü61a and transcriptional analysis of genes involved in quinaldine degradation. J Bacteriol 189:3855–3867
Reizer A, Deutscher J, Saier MH, Reizer J (1991) Analysis of the gluconate (gnt) operon of Bacillus subtilis. Mol Microbiol 5:1081–1089
Sachelaru P, Schiltz E, Igloi GL, Brandsch R (2005) An α/β -fold C-C bond hydrolase is involved in a central step of nicotine catabolism by Arthrobacter nicotinovorans. J Bacteriol 187:8516–8519
Sachelaru P, Schiltz E, Brandsch R (2006) A functional mobA gene for molybdopterin cytosine dinucleotide cofactor biosynthesis is required for activity and holoenzyme assembly of the heterotrimeric nicotine dehydrogenase of Arthrobacter nicotinovorans. Appl Environ Microbiol 72:5126–5131
Sandu C, Chiribau C-B, Brandsch R (2003) Characterization of HdnoR, the transcriptional repressor of the 6-hydroxy- d -nicotine oxidase gene of Arthrobacter nicotinovorans pAO1, and its DNA-binding activity in response to l- and d- nicotine derivatives. J Biol Chem 278: 51307–51315
Schleberger C, Sachelaru P, Brandsch R, Schulz GE (2007) Structure and action of a C—C bond cleaving α/β-hydrolase involved in nicotine degradation. J Mol Biol 367:409–418
Schmitz J, Wuebbens MM, Rajagopalan KV, Leimkühler S (2007) Role of the C-terminal Gly-Gly motif of Escherichia coli MoaD, a molybdenum cofactor biosynthesis protein with a ubiquitin fold. Biochem 46:909–916
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2009 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Ganas, P., Igloi, G.L., Brandsch, R. (2009). The Megaplasmid pAO1 of Arthrobacter Nicotinovorans and Nicotine Catabolism. In: Schwartz, E. (eds) Microbial Megaplasmids. Microbiology Monographs, vol 11. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-85467-8_12
Download citation
DOI: https://doi.org/10.1007/978-3-540-85467-8_12
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-85466-1
Online ISBN: 978-3-540-85467-8
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)