Proteomic study of linuron and 3,4-dichloroaniline degradation by Variovorax sp. WDL1: evidence for the involvement of an aniline dioxygenase-related multicomponent protein - 2010
Proteomic study of linuron and 3,4-dichloroaniline degradation by Variovorax sp. WDL1: evidence for the involvement of an aniline dioxygenase-related multicomponent protein
[en] A proteomic approach was used to explore the metabolism of the phenylurea herbicide linuron and 3,4-dichloroaniline (3,4-DCA) in Variovorax sp. WDL1. This bacterium grows on linuron as sole source of carbon, nitrogen and energy, while it transiently accumulates 3,4-DCA as a metabolite. Differential protein expression analysis of Variovorax sp. WDL1 grown in a heterotrophic medium in the presence and absence of linuron or 3,4-DCA was conducted using 2-D PAGE. Selected up- and downregulated proteins were identified with nanoLC-ESI-MS/MS. In the 3,4-DCA-supplemented culture, upregulation of several proteins showing high amino acid sequence similarity to different components of the multicomponent aniline dioxygenase in aniline-degrading Proteobacteria was observed. For one of the components, multiple variant proteins were detected, suggesting that strain WDL1 harbors several copies of the aniline dioxygenase (AD) gene cluster which are simultaneously expressed in the presence of 3,4-DCA. A number of unidentifiable proteins, which were upregulated in the linuron- and/or 3,4-DCA-supplemented cultures, might represent up to now uncharacterized proteins with a role in linuron and/or 3,4-DCA degradation in strain WDL1. In addition, several stress-related proteins were differentially expressed.
Leroy, Baptiste ; Université de Mons > Faculté des Sciences > Protéomie et Microbiologie
Wattiez, Ruddy ; Université de Mons > Faculté des Sciences > Protéomie et Microbiologie
Schoofs, G.
De Mot, R.
Springael, D.
Language :
English
Title :
Proteomic study of linuron and 3,4-dichloroaniline degradation by Variovorax sp. WDL1: evidence for the involvement of an aniline dioxygenase-related multicomponent protein
Ang E.L., Obbard J.P., Zhao H. Probing the molecular determinants of aniline dioxygenase substrate specificity by saturation mutagenesis. FEBS J. 2007, 274:928-939.
Batisson I., Pesce S., Besse-Hoggan P., Sancelme M., Bohatier J. Isolation and characterization of diuron-degrading bacteria from lotic surface water. Microb. Ecol. 2007, 54:761-770.
Boon N., Goris J., De Vos P., Verstraete W., Top E.M. Genetic diversity among the 3-chloroaniline- and aniline-degrading strains of the Comamonadaceae. Appl. Environ. Microbiol. 2001, 67:1107-1115.
Breugelmans P., Barken K.B., Tolker-Nielsen T., Hofkens J., Dejonghe W., Springael D. Architecture and spatial organization in a triple-species bacterial biofilm synergistically degrading the phenylurea herbicide linuron. FEMS Microbiol. Ecol. 2008, 64:271-282.
Breugelmans P., D'Huys P.-J., De Mot R., Springael D. Characterization of novel linuron-mineralizing bacterial consortia enriched from long-term linuron-treated agricultural soils. FEMS Microbiol. Ecol. 2007, 62:374-385.
Caux P.Y., Kent R.A., Fan G.T., Grande C. Canadian water guidelines for linuron. Environ. Toxicol. Water Qual. 1998, 13:1-41.
Chistoserdova L., Vorholt J.A., Thauer R.K., Lidstrom M.E. C1 transfer enzymes and coenzymes linking methylotrophic bacteria and methanogenic archaea. Science 1998, 281:99-102.
Cullington J.E., Walker A. Rapid biodegradation of diuron and other phenylurea herbicides by a soil bacterium. Soil Biol. Biochem. 1999, 31:677-686.
Dejonghe, W., 2003. The importance of genetic and metabolic interactions between bacteria in the degradation of herbicides. Ph.D. thesis, University of Ghent, Belgium.
Dejonghe W., Berteloot E., Goris J., Boon N., Crul K., Maertens S., Höfte M., De Vos P., Verstraete W., Top E.M. Synergistic degradation of linuron by a bacterial consortium and isolation of a single linuron-degrading Variovorax strain. Appl. Environ. Microbiol. 2003, 69:1532-1541.
De Mot R., Schoofs G., Nagy I. Proteome analysis of Streptomyces coelicolor mutants affected in the proteasome system reveals changes in stress-responsive proteins. Arch. Microbiol. 2007, 188:257-271.
De Mot R., Vanderleyden J. Application of two-dimensional protein analysis for strain fingerprinting and mutant analysis of Azospirillum species. Can. J. Microbiol. 1989, 35:960-967.
Domínguez-Cuevas P., González-Pastor J.-E., Marqués S., Ramos J.-L., de Lorenzo V. Transcriptional tradeoff between metabolic and stress-response programs in Pseudomonas putida KT2440 cells exposed to toluene. J. Biol. Chem. 2006, 281:11981-11991.
Engelhardt G., Wallnöfer P.R., Plapp R. Identification of N,O-dimethylhydroxylamine as a microbial degradation product of the herbicide, linuron. Appl. Microbiol. 1972, 23:664-666.
Engelhardt G., Wallnöfer P.R., Plapp R. Purification and properties of an aryl acylamidase of Bacillus sphaericus, catalyzing the hydrolysis of various phenylamide herbicides and fungicides. Appl. Environ. Microbiol. 1973, 26:709-718.
Fujii T., Takeo M., Maeda Y. Plasmid-encoded genes specifying aniline oxidation from Acinetobacter sp. YAA. Microbiology 1997, 143:93-99.
Fukumori F., Saint C.P. Nucleotide sequences and regulational analysis of genes involved in conversion of aniline to catechol in Pseudomonas putida UCC22(pTN1). J. Bacteriol. 1997, 179:399-408.
Gottesman S., Wickner S., Maurizi M.R. Protein quality control: triage by chaperones and proteases. Genes Dev. 1997, 11:815-823.
Hernando M.D., Ejerhoon M., Fernández-Alba A.R., Chisti Y. Combined toxicity effects of MTBE and pesticides measured with Vibrio fischeri and Daphnia magna bioassays. Water Res. 2003, 37:4091-4098.
Jeannot M.A., Zheng J., Li L. Observation of sodium gel-induced protein modifications in sodium dodecyl sulfate polyacrylamide gel electrophoresis and its implications for accurate molecular weight determination of gel-separated proteins by matrix-assisted laser desorption ionization time-of-flight mass spectrometry. J. Am. Soc. Mass Spectr. 1999, 10:512-520.
Kegley S., Hill B., Orme S., Choi A.H. PAN Pesticide Database 2008, Pesticide Action Network North America, San Francisco, CA, URL:. http://www.pesticideinfo.org.
Kim H.J., Kim S.E., Kim J.G., Kim J.C., Choi G.J., Kim H.T., Hwang I., Kim H.G., Cho K.Y., Lee S.-W. Cloning genes involved in aniline degradation from Delftia acidovorans. Kor. J. Microbiol. Biotechnol. 2003, 31:25-31.
Kim Y.M., Park K., Kim W.C., Shin J.H., Kim J.E., Park H.D., Rhee I.K. Cloning and characterization of a catechol-degrading gene cluster from 3,4-dichloroaniline degrading bacterium Pseudomonas sp. KB35B. J. Agric. Food Chem. 2007, 55:4722-4727.
Kumar S., Tamura K., Nei M. MEGA 3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief Bioinform. 2004, 5:150-163.
Liang Q., Takeo M., Chen M., Zhang W., Xu Y., Lin M. Chromosome-encoded gene cluster for the metabolic pathway that converts aniline to TCA-cycle intermediates in Delftia tsuruhatensis AD9. Microbiology 2005, 151:3435-3446.
McIntyre B.S., Barlow N.J., Foster P.M. Male rats exposed to linuron in utero exhibit permanent changes in anogenital distance, nipple retention, and epididymal malformations that result in subsequent testicular atrophy. Toxicol. Sci. 2002, 65:62-70.
Murakami S., Hayashi T., Maeda T., Takenaka S., Aoki K. Cloning and functional analysis of aniline dioxygenase gene cluster, from Frateuria sp. ANA-18, that metabolizes aniline via an ortho-cleavage pathway of catechol. Biosci. Biotechnol. Biochem. 2003, 67:2351-2358.
Narberhaus F. Negative regulation of bacterial heat shock genes. Mol. Microbiol. 1999, 31:1-8.
Noël-Georis I., Vallaeys T., Chauvaux R., Monchy S., Falmagne P., Mergeay M., Wattiez R. Global analysis of the Ralstonia metallidurans proteome: prelude for the large-scale study of heavy metal response. Proteomics 2004, 4:151-179.
Perkins D.N., Pappin D.J.C., Creasy D.M., Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20:3551-3567.
Segura A., Godoy P., van Dillewijn P., Hurtado A., Arroyo N., Santacruz S., Ramos J.-L. Proteomic analysis reveals the participation of energy- and stress-related proteins in the response of Pseudomonas putida DOT-T1E to toluene. J. Bacteriol. 2005, 187:5937-5945.
Servant P., Mazodier O. Negative regulation of the heat shock response in Streptomyces. Arch. Microbiol. 2001, 176:237-242.
Sørensen S.R., Rasmussen J., Jacobsen C.S., Jacobsen O.S., Juhler R.K., Aamand J. Elucidating the key member of a linuron-mineralizing bacterial community by PCR and reverse transcription-PCR denaturing gradient gel electrophoresis 16S rRNA gene fingerprinting and cultivation. Appl. Environ. Microbiol. 2005, 71:4144-4148.
Takeo M., Fujii T., Maeda Y. Sequence analysis of the genes encoding a multicomponent dioxygenase involved in oxidation of aniline and o-toluidine in Acinetobacter sp. YAA. J. Ferment. Bioeng. 1998, 85:17-24.
Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994, 22:4673-4680.
Tixier C., Sancelme M., Aït-Aïssa S., Widehem P., Bonnemoy F., Cuer A., Truffaut N., Veschambre H. Biotransformation of phenylurea herbicides by a soil bacterial strain, Arthrobacter sp. N2: structure, ecotoxicity and fate of diuron metabolite with soil fungi. Chemosphere 2002, 46:519-526.
Travkin V.M., Solyanikova I.P., Rietjens I.M.C.M., Vervoort J., van Berkel W.J.H., Golovleva L.A. Degradation of 3,4-dichloro- and 3,4-difluoroaniline by Pseudomonas fluorescens 26-K. J. Environ. Sci. Health B 2003, 38:121-132.
Turnbull G.A., Ousley M., Walker A., Shaw E., Morgan J.A.W. Degradation of substituted phenylurea herbicides by Arthrobacter globiformis D47 and characterization of a plasmid-associated hydrolase gene, puhA. Appl. Environ. Microbiol. 2001, 67:2270-2275.
Urata M., Uchida E., Nojiri H., Omori T., Obo R., Miyaura N., Ouchiyama N. Genes involved in aniline degradation by Delftia acidovorans strain 7N and its distribution in the natural environment. Biosci. Biotechnol. Biochem. 2004, 68:2457-2465.
Vangnai A.S., Petchkroh W. Biodegradation of 4-chloroaniline by bacteria enriched from soil. FEMS Microbiol. Lett. 2007, 268:209-216.
von Mering C., Jensen L.J., Kuhn M., Chaffron S., Doerks T., Krüger B., Snel B., Bork P. STRING 7 - recent developments in the integration and prediction of protein interactions. Nucleic Acids Res. 2007, 35:D358-D362.
Wallnöfer P.R. The decomposition of urea herbicides by Bacillus sphaericus, isolated from soil. Weed Res. 1969, 9:333-339.
Wilkins M.R., Gasteiger E., Gooley A.A., Herbert B.R., Molloy M.P., Binz P.-A., Ou K., Sanchez J.-C., Bairoch A., Williams K.L., Hochstrasser D.F. High-throughput mass spectrometric discovery of protein post-translational modifications. J. Mol. Biol. 1999, 289:645-657.
You I.S., Bartha R. Metabolism of 3,4-dichloroaniline by Pseudomonas putida. J. Agric. Food Chem. 1982, 30:274-277.
