Abstract
Pseudomonas putida F1 utilizes p-cymene (p-isopropyltoluene) by an 11-step pathway through p-cumate (p-isopropylbenzoate) to isobutyrate, pyruvate, and acetyl coenzyme A. The cym operon, encoding the conversion of p-cymene to p-cumate, is located just upstream of the cmt operon, which encodes the further catabolism of p-cumate and is located, in turn, upstream of the tod (toluene catabolism) operon in P. putida F1. The sequences of an 11,236-bp DNA segment carrying the cym operon and a 915-bp DNA segment completing the sequence of the 2,673-bp DNA segment separating the cmt and tod operons have been determined and are discussed here. The cym operon contains six genes in the order cymBCAaAbDE. The gene products have been identified both by functional assays and by comparing deduced amino acid sequences to published sequences. Thus, cymAa and cymAb encode the two components of p-cymene monooxygenase, a hydroxylase and a reductase, respectively; cymB encodes p-cumic alcohol dehydrogenase; cymC encodes p-cumic aldehyde dehydrogenase; cymD encodes a putative outer membrane protein related to gene products of other aromatic hydrocarbon catabolic operons, but having an unknown function in p-cymene catabolism; and cymE encodes an acetyl coenzyme A synthetase whose role in this pathway is also unknown. Upstream of the cym operon is a regulatory gene, cymR. By using recombinant bacteria carrying either the operator-promoter region of the cym operon or the cmt operon upstream of genes encoding readily assayed enzymes, in the presence or absence of cymR, it was demonstrated that cymR encodes a repressor which controls expression of both the cym and cmt operons and is inducible by p-cumate but not p-cymene. Short (less than 350 bp) homologous DNA segments that are located upstream of cymR and between the cmt and tod operons may have been involved in recombination events that led to the current arrangement of cym, cmt, and tod genes in P. putida F1.
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- Alting-Mees M. A., Short J. M. pBluescript II: gene mapping vectors. Nucleic Acids Res. 1989 Nov 25;17(22):9494–9494. doi: 10.1093/nar/17.22.9494. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Altschul S. F., Gish W., Miller W., Myers E. W., Lipman D. J. Basic local alignment search tool. J Mol Biol. 1990 Oct 5;215(3):403–410. doi: 10.1016/S0022-2836(05)80360-2. [DOI] [PubMed] [Google Scholar]
- Assinder S. J., Williams P. A. The TOL plasmids: determinants of the catabolism of toluene and the xylenes. Adv Microb Physiol. 1990;31:1–69. doi: 10.1016/s0065-2911(08)60119-8. [DOI] [PubMed] [Google Scholar]
- Babbitt P. C., Kenyon G. L., Martin B. M., Charest H., Slyvestre M., Scholten J. D., Chang K. H., Liang P. H., Dunaway-Mariano D. Ancestry of the 4-chlorobenzoate dehalogenase: analysis of amino acid sequence identities among families of acyl:adenyl ligases, enoyl-CoA hydratases/isomerases, and acyl-CoA thioesterases. Biochemistry. 1992 Jun 23;31(24):5594–5604. doi: 10.1021/bi00139a024. [DOI] [PubMed] [Google Scholar]
- Barnsley E. A. Metabolism of 2,6-dimethylnaphthalene by flavobacteria. Appl Environ Microbiol. 1988 Feb;54(2):428–433. doi: 10.1128/aem.54.2.428-433.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bennett V. Ankyrins. Adaptors between diverse plasma membrane proteins and the cytoplasm. J Biol Chem. 1992 May 5;267(13):8703–8706. [PubMed] [Google Scholar]
- Bennett V. Spectrin-based membrane skeleton: a multipotential adaptor between plasma membrane and cytoplasm. Physiol Rev. 1990 Oct;70(4):1029–1065. doi: 10.1152/physrev.1990.70.4.1029. [DOI] [PubMed] [Google Scholar]
- Benson D., Lipman D. J., Ostell J. GenBank. Nucleic Acids Res. 1993 Jul 1;21(13):2963–2965. doi: 10.1093/nar/21.13.2963. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Black P. N. Primary sequence of the Escherichia coli fadL gene encoding an outer membrane protein required for long-chain fatty acid transport. J Bacteriol. 1991 Jan;173(2):435–442. doi: 10.1128/jb.173.2.435-442.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Blattner F. R., Burland V., Plunkett G., 3rd, Sofia H. J., Daniels D. L. Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes. Nucleic Acids Res. 1993 Nov 25;21(23):5408–5417. doi: 10.1093/nar/21.23.5408. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brennan R. G., Matthews B. W. The helix-turn-helix DNA binding motif. J Biol Chem. 1989 Feb 5;264(4):1903–1906. [PubMed] [Google Scholar]
- Brown T. D., Jones-Mortimer M. C., Kornberg H. L. The enzymic interconversion of acetate and acetyl-coenzyme A in Escherichia coli. J Gen Microbiol. 1977 Oct;102(2):327–336. doi: 10.1099/00221287-102-2-327. [DOI] [PubMed] [Google Scholar]
- Chang A. C., Cohen S. N. Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid. J Bacteriol. 1978 Jun;134(3):1141–1156. doi: 10.1128/jb.134.3.1141-1156.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Chang C., Yoshida A. Cloning and characterization of the gene encoding mouse mitochondrial aldehyde dehydrogenase. Gene. 1994 Oct 21;148(2):331–336. doi: 10.1016/0378-1119(94)90708-0. [DOI] [PubMed] [Google Scholar]
- DAGLEY S., PATEL M. D. Oxidation of p-cresol and related compounds by a Pseudomonas. Biochem J. 1957 Jun;66(2):227–233. doi: 10.1042/bj0660227. [DOI] [PMC free article] [PubMed] [Google Scholar]
- DAVIS J. B., RAYMOND R. L. Oxidation of alkyl-substituted cyclic hydrocarbons by a Nocardia during growth on n-alkanes. Appl Microbiol. 1961 Sep;9:383–388. doi: 10.1128/am.9.5.383-388.1961. [DOI] [PMC free article] [PubMed] [Google Scholar]
- DeFrank J. J., Ribbons D. W. p-Cymene pathway in Pseudomonas putida: ring cleavage of 2,3-dihydroxy-p-cumate and subsequent reactions. J Bacteriol. 1977 Mar;129(3):1365–1374. doi: 10.1128/jb.129.3.1365-1374.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- DeFrank J. J., Ribbons D. W. p-cymene pathway in Pseudomonas putida: initial reactions. J Bacteriol. 1977 Mar;129(3):1356–1364. doi: 10.1128/jb.129.3.1356-1364.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Defrank J. J., Ribbons D. W. The p-cymene pathway in Pseudomonas putida PL: isolation of a dihydrodiol accumulated by a mutant. Biochem Biophys Res Commun. 1976 Jun 21;70(4):1129–1135. doi: 10.1016/0006-291x(76)91020-2. [DOI] [PubMed] [Google Scholar]
- DiGate R. J., Marians K. J. Molecular cloning and DNA sequence analysis of Escherichia coli topB, the gene encoding topoisomerase III. J Biol Chem. 1989 Oct 25;264(30):17924–17930. [PubMed] [Google Scholar]
- Dretzen G., Bellard M., Sassone-Corsi P., Chambon P. A reliable method for the recovery of DNA fragments from agarose and acrylamide gels. Anal Biochem. 1981 Apr;112(2):295–298. doi: 10.1016/0003-2697(81)90296-7. [DOI] [PubMed] [Google Scholar]
- Eaton R. W., Chapman P. J. Formation of indigo and related compounds from indolecarboxylic acids by aromatic acid-degrading bacteria: chromogenic reactions for cloning genes encoding dioxygenases that act on aromatic acids. J Bacteriol. 1995 Dec;177(23):6983–6988. doi: 10.1128/jb.177.23.6983-6988.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Eaton R. W., Karns J. S. Cloning and analysis of s-triazine catabolic genes from Pseudomonas sp. strain NRRLB-12227. J Bacteriol. 1991 Feb;173(3):1215–1222. doi: 10.1128/jb.173.3.1215-1222.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Eaton R. W. Organization and evolution of naphthalene catabolic pathways: sequence of the DNA encoding 2-hydroxychromene-2-carboxylate isomerase and trans-o-hydroxybenzylidenepyruvate hydratase-aldolase from the NAH7 plasmid. J Bacteriol. 1994 Dec;176(24):7757–7762. doi: 10.1128/jb.176.24.7757-7762.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Eaton R. W., Ribbons D. W. Metabolism of dibutylphthalate and phthalate by Micrococcus sp. strain 12B. J Bacteriol. 1982 Jul;151(1):48–57. doi: 10.1128/jb.151.1.48-57.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Eaton R. W., Timmis K. N. Characterization of a plasmid-specified pathway for catabolism of isopropylbenzene in Pseudomonas putida RE204. J Bacteriol. 1986 Oct;168(1):123–131. doi: 10.1128/jb.168.1.123-131.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Eaton R. W. p-Cumate catabolic pathway in Pseudomonas putida Fl: cloning and characterization of DNA carrying the cmt operon. J Bacteriol. 1996 Mar;178(5):1351–1362. doi: 10.1128/jb.178.5.1351-1362.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fox B. G., Shanklin J., Ai J., Loehr T. M., Sanders-Loehr J. Resonance Raman evidence for an Fe-O-Fe center in stearoyl-ACP desaturase. Primary sequence identity with other diiron-oxo proteins. Biochemistry. 1994 Nov 1;33(43):12776–12786. doi: 10.1021/bi00209a008. [DOI] [PubMed] [Google Scholar]
- Gibson D. T., Koch J. R., Kallio R. E. Oxidative degradation of aromatic hydrocarbons by microorganisms. I. Enzymatic formation of catechol from benzene. Biochemistry. 1968 Jul;7(7):2653–2662. doi: 10.1021/bi00847a031. [DOI] [PubMed] [Google Scholar]
- Grunstein M., Hogness D. S. Colony hybridization: a method for the isolation of cloned DNAs that contain a specific gene. Proc Natl Acad Sci U S A. 1975 Oct;72(10):3961–3965. doi: 10.1073/pnas.72.10.3961. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Habe H., Kasuga K., Nojiri H., Yamane H., Omori T. Analysis of cumene (isopropylbenzene) degradation genes from Pseudomonas fluorescens IP01. Appl Environ Microbiol. 1996 Dec;62(12):4471–4477. doi: 10.1128/aem.62.12.4471-4477.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hall R. M., Stokes H. W. Integrons: novel DNA elements which capture genes by site-specific recombination. Genetica. 1993;90(2-3):115–132. doi: 10.1007/BF01435034. [DOI] [PubMed] [Google Scholar]
- Harayama S., Leppik R. A., Rekik M., Mermod N., Lehrbach P. R., Reineke W., Timmis K. N. Gene order of the TOL catabolic plasmid upper pathway operon and oxidation of both toluene and benzyl alcohol by the xylA product. J Bacteriol. 1986 Aug;167(2):455–461. doi: 10.1128/jb.167.2.455-461.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Harayama S., Rekik M., Wubbolts M., Rose K., Leppik R. A., Timmis K. N. Characterization of five genes in the upper-pathway operon of TOL plasmid pWW0 from Pseudomonas putida and identification of the gene products. J Bacteriol. 1989 Sep;171(9):5048–5055. doi: 10.1128/jb.171.9.5048-5055.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hempel J., Nicholas H., Lindahl R. Aldehyde dehydrogenases: widespread structural and functional diversity within a shared framework. Protein Sci. 1993 Nov;2(11):1890–1900. doi: 10.1002/pro.5560021111. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Herrmann H., Müller C., Schmidt I., Mahnke J., Petruschka L., Hahnke K. Localization and organization of phenol degradation genes of Pseudomonas putida strain H. Mol Gen Genet. 1995 Apr 20;247(2):240–246. doi: 10.1007/BF00705655. [DOI] [PubMed] [Google Scholar]
- Inoue J., Shaw J. P., Rekik M., Harayama S. Overlapping substrate specificities of benzaldehyde dehydrogenase (the xylC gene product) and 2-hydroxymuconic semialdehyde dehydrogenase (the xylG gene product) encoded by TOL plasmid pWW0 of Pseudomonas putida. J Bacteriol. 1995 Mar;177(5):1196–1201. doi: 10.1128/jb.177.5.1196-1201.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S. Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome. DNA Res. 1995 Aug 31;2(4):153-66, 191-8. doi: 10.1093/dnares/2.4.153. [DOI] [PubMed] [Google Scholar]
- Karplus P. A., Walsh K. A., Herriott J. R. Amino acid sequence of spinach ferredoxin:NADP+ oxidoreductase. Biochemistry. 1984 Dec 18;23(26):6576–6583. doi: 10.1021/bi00321a046. [DOI] [PubMed] [Google Scholar]
- Khramtsov N. V., Blunt D. S., Montelone B. A., Upton S. J. The putative acetyl-CoA synthetase gene of Cryptosporidium parvum and a new conserved protein motif in acetyl-CoA synthetases. J Parasitol. 1996 Jun;82(3):423–427. [PubMed] [Google Scholar]
- Klotz M. G., Anderson A. J. Sequence of a gene encoding periplasmic Pseudomonas syringae ankyrin. Gene. 1995 Oct 16;164(1):187–188. doi: 10.1016/0378-1119(95)00482-l. [DOI] [PubMed] [Google Scholar]
- Kok M., Oldenhuis R., van der Linden M. P., Raatjes P., Kingma J., van Lelyveld P. H., Witholt B. The Pseudomonas oleovorans alkane hydroxylase gene. Sequence and expression. J Biol Chem. 1989 Apr 5;264(10):5435–5441. [PubMed] [Google Scholar]
- Madhyastha K. M., Rangachari P. N., Raghabendra Rao M., Bhattacharyya P. K. Microbiological transformations of terpenes. XV. Enzyme systems in the catabolism of p-cymene in PL-strain. Indian J Biochem. 1968 Dec;5(4):167–173. [PubMed] [Google Scholar]
- Margolin W., Bramhill D., Long S. R. The dnaA gene of Rhizobium meliloti lies within an unusual gene arrangement. J Bacteriol. 1995 May;177(10):2892–2900. doi: 10.1128/jb.177.10.2892-2900.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Martin R. R., Marshall V. D., Sokatch J. R., Unger L. Common enzymes of branched-chain amino acid catabolism in Pseudomonas putida. J Bacteriol. 1973 Jul;115(1):198–204. doi: 10.1128/jb.115.1.198-204.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mason J. R., Cammack R. The electron-transport proteins of hydroxylating bacterial dioxygenases. Annu Rev Microbiol. 1992;46:277–305. doi: 10.1146/annurev.mi.46.100192.001425. [DOI] [PubMed] [Google Scholar]
- Minami-Ishii N., Taketani S., Osumi T., Hashimoto T. Molecular cloning and sequence analysis of the cDNA for rat mitochondrial enoyl-CoA hydratase. Structural and evolutionary relationships linked to the bifunctional enzyme of the peroxisomal beta-oxidation system. Eur J Biochem. 1989 Oct 20;185(1):73–78. doi: 10.1111/j.1432-1033.1989.tb15083.x. [DOI] [PubMed] [Google Scholar]
- Miyachi N., Tanaka T., Suzuki T., Hotta Y., Omori T. Microbial oxidation of dimethylnaphthalene isomers. Appl Environ Microbiol. 1993 May;59(5):1504–1506. doi: 10.1128/aem.59.5.1504-1506.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Munson R., Jr, Grass S. Purification, cloning, and sequence of outer membrane protein P1 of Haemophilus influenzae type b. Infect Immun. 1988 Sep;56(9):2235–2242. doi: 10.1128/iai.56.9.2235-2242.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nakagawa J., Waldner H., Meyer-Monard S., Hofsteenge J., Jenö P., Moroni C. AUH, a gene encoding an AU-specific RNA binding protein with intrinsic enoyl-CoA hydratase activity. Proc Natl Acad Sci U S A. 1995 Mar 14;92(6):2051–2055. doi: 10.1073/pnas.92.6.2051. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Needleman S. B., Wunsch C. D. A general method applicable to the search for similarities in the amino acid sequence of two proteins. J Mol Biol. 1970 Mar;48(3):443–453. doi: 10.1016/0022-2836(70)90057-4. [DOI] [PubMed] [Google Scholar]
- Neidle E. L., Hartnett C., Ornston L. N., Bairoch A., Rekik M., Harayama S. Nucleotide sequences of the Acinetobacter calcoaceticus benABC genes for benzoate 1,2-dioxygenase reveal evolutionary relationships among multicomponent oxygenases. J Bacteriol. 1991 Sep;173(17):5385–5395. doi: 10.1128/jb.173.17.5385-5395.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Neumann-Spallart C., Brandtner M., Kraus M., Jakowitsch J., Bayer M. G., Maier T. L., Schenk H. E., Löffelhardt W. The petFI gene encoding ferredoxin I is located close to the str operon on the cyanelle genome of Cyanophora paradoxa. FEBS Lett. 1990 Jul 30;268(1):55–58. doi: 10.1016/0014-5793(90)80971-k. [DOI] [PubMed] [Google Scholar]
- O'Connor C. D., Humphreys G. O. Expression of the Eco RI restriction-modification system and the construction of positive-selection cloning vectors. Gene. 1982 Dec;20(2):219–229. doi: 10.1016/0378-1119(82)90041-5. [DOI] [PubMed] [Google Scholar]
- Oliver D. Protein secretion in Escherichia coli. Annu Rev Microbiol. 1985;39:615–648. doi: 10.1146/annurev.mi.39.100185.003151. [DOI] [PubMed] [Google Scholar]
- Pan W., Spratt B. G. Regulation of the permeability of the gonococcal cell envelope by the mtr system. Mol Microbiol. 1994 Feb;11(4):769–775. doi: 10.1111/j.1365-2958.1994.tb00354.x. [DOI] [PubMed] [Google Scholar]
- Persson B., Krook M., Jörnvall H. Characteristics of short-chain alcohol dehydrogenases and related enzymes. Eur J Biochem. 1991 Sep 1;200(2):537–543. doi: 10.1111/j.1432-1033.1991.tb16215.x. [DOI] [PubMed] [Google Scholar]
- Porter T. D., Kasper C. B. NADPH-cytochrome P-450 oxidoreductase: flavin mononucleotide and flavin adenine dinucleotide domains evolved from different flavoproteins. Biochemistry. 1986 Apr 8;25(7):1682–1687. doi: 10.1021/bi00355a036. [DOI] [PubMed] [Google Scholar]
- Raymond R. L., Jamison V. W., Hudson J. O. Microbial hydrocarbon co-oxidation. I. Oxidation of mono- and dicyclic hydrocarbons by soil isolates of the genus Nocardia. Appl Microbiol. 1967 Jul;15(4):857–865. doi: 10.1128/am.15.4.857-865.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Reid M. F., Fewson C. A. Molecular characterization of microbial alcohol dehydrogenases. Crit Rev Microbiol. 1994;20(1):13–56. doi: 10.3109/10408419409113545. [DOI] [PubMed] [Google Scholar]
- Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Saraste M., Sibbald P. R., Wittinghofer A. The P-loop--a common motif in ATP- and GTP-binding proteins. Trends Biochem Sci. 1990 Nov;15(11):430–434. doi: 10.1016/0968-0004(90)90281-f. [DOI] [PubMed] [Google Scholar]
- Shanklin J., Whittle E., Fox B. G. Eight histidine residues are catalytically essential in a membrane-associated iron enzyme, stearoyl-CoA desaturase, and are conserved in alkane hydroxylase and xylene monooxygenase. Biochemistry. 1994 Nov 1;33(43):12787–12794. doi: 10.1021/bi00209a009. [DOI] [PubMed] [Google Scholar]
- Shaw J. P., Harayama S. Purification and characterisation of TOL plasmid-encoded benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase of Pseudomonas putida. Eur J Biochem. 1990 Aug 17;191(3):705–714. doi: 10.1111/j.1432-1033.1990.tb19179.x. [DOI] [PubMed] [Google Scholar]
- Shaw J. P., Harayama S. Purification and characterisation of the NADH:acceptor reductase component of xylene monooxygenase encoded by the TOL plasmid pWW0 of Pseudomonas putida mt-2. Eur J Biochem. 1992 Oct 1;209(1):51–61. doi: 10.1111/j.1432-1033.1992.tb17260.x. [DOI] [PubMed] [Google Scholar]
- Shaw J. P., Rekik M., Schwager F., Harayama S. Kinetic studies on benzyl alcohol dehydrogenase encoded by TOL plasmid pWWO. A member of the zinc-containing long chain alcohol dehydrogenase family. J Biol Chem. 1993 May 25;268(15):10842–10850. [PubMed] [Google Scholar]
- Shen Z., Byers D. M. Isolation of Vibrio harveyi acyl carrier protein and the fabG, acpP, and fabF genes involved in fatty acid biosynthesis. J Bacteriol. 1996 Jan;178(2):571–573. doi: 10.1128/jb.178.2.571-573.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Simon M. J., Osslund T. D., Saunders R., Ensley B. D., Suggs S., Harcourt A., Suen W. C., Cruden D. L., Gibson D. T., Zylstra G. J. Sequences of genes encoding naphthalene dioxygenase in Pseudomonas putida strains G7 and NCIB 9816-4. Gene. 1993 May 15;127(1):31–37. doi: 10.1016/0378-1119(93)90613-8. [DOI] [PubMed] [Google Scholar]
- Suzuki M., Hayakawa T., Shaw J. P., Rekik M., Harayama S. Primary structure of xylene monooxygenase: similarities to and differences from the alkane hydroxylation system. J Bacteriol. 1991 Mar;173(5):1690–1695. doi: 10.1128/jb.173.5.1690-1695.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wang Y., Rawlings M., Gibson D. T., Labbé D., Bergeron H., Brousseau R., Lau P. C. Identification of a membrane protein and a truncated LysR-type regulator associated with the toluene degradation pathway in Pseudomonas putida F1. Mol Gen Genet. 1995 Mar 10;246(5):570–579. doi: 10.1007/BF00298963. [DOI] [PubMed] [Google Scholar]
- Wheelis L. The genetics of dissimilarity pathways in Pseudomonas. Annu Rev Microbiol. 1975;29:505–524. doi: 10.1146/annurev.mi.29.100175.002445. [DOI] [PubMed] [Google Scholar]
- Wierenga R. K., Terpstra P., Hol W. G. Prediction of the occurrence of the ADP-binding beta alpha beta-fold in proteins, using an amino acid sequence fingerprint. J Mol Biol. 1986 Jan 5;187(1):101–107. doi: 10.1016/0022-2836(86)90409-2. [DOI] [PubMed] [Google Scholar]
- Wilbur W. J., Lipman D. J. Rapid similarity searches of nucleic acid and protein data banks. Proc Natl Acad Sci U S A. 1983 Feb;80(3):726–730. doi: 10.1073/pnas.80.3.726. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wyndham R. C., Cashore A. E., Nakatsu C. H., Peel M. C. Catabolic transposons. Biodegradation. 1994 Dec;5(3-4):323–342. doi: 10.1007/BF00696468. [DOI] [PubMed] [Google Scholar]
- Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene. 1985;33(1):103–119. doi: 10.1016/0378-1119(85)90120-9. [DOI] [PubMed] [Google Scholar]
- Yeh W. K., Gibson D. T., Liu T. N. Toluene dioxygenase: a multicomponent enzyme system. Biochem Biophys Res Commun. 1977 Sep 9;78(1):401–410. doi: 10.1016/0006-291x(77)91268-2. [DOI] [PubMed] [Google Scholar]
- Zylstra G. J., Gibson D. T. Toluene degradation by Pseudomonas putida F1. Nucleotide sequence of the todC1C2BADE genes and their expression in Escherichia coli. J Biol Chem. 1989 Sep 5;264(25):14940–14946. [PubMed] [Google Scholar]
- Zylstra G. J., McCombie W. R., Gibson D. T., Finette B. A. Toluene degradation by Pseudomonas putida F1: genetic organization of the tod operon. Appl Environ Microbiol. 1988 Jun;54(6):1498–1503. doi: 10.1128/aem.54.6.1498-1503.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
- van Beilen J. B., Penninga D., Witholt B. Topology of the membrane-bound alkane hydroxylase of Pseudomonas oleovorans. J Biol Chem. 1992 May 5;267(13):9194–9201. [PubMed] [Google Scholar]