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. 1988 Mar;170(3):1297–1304. doi: 10.1128/jb.170.3.1297-1304.1988

Transcriptional regulation, nucleotide sequence, and localization of the promoter of the catBC operon in Pseudomonas putida.

T L Aldrich 1, A M Chakrabarty 1
PMCID: PMC210906  PMID: 2449420

Abstract

The catB and catC genes encode cis,cis-muconate lactonizing enzyme I (EC 5.5.1.1) and muconolactone isomerase (EC 5.3.3.4), respectively. These enzymes are required for the dissimilation of benzoate to beta-ketoadipate by Pseudomonas putida and are under coordinate transcriptional regulation. By deletion analysis and the use of pKT240 as a promoter probe vector, we located a single promoter region for the catBC operon upstream of catB. RNA-DNA hybridization studies, together with reverse transcriptase mapping, demonstrated that this promoter must be activated in the presence of an inducer molecule for effective transcription of the operon. In addition, the transcription initiation site was located 64 base pairs upstream of the catB initiation codon, and sequences upstream of -43 were required for promoter function. The catBC promoter was compared with other positively regulated procaryotic promoters to identify possible consensus sequences.

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Selected References

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  1. Aldrich T. L., Frantz B., Gill J. F., Kilbane J. J., Chakrabarty A. M. Cloning and complete nucleotide sequence determination of the catB gene encoding cis,cis-muconate lactonizing enzyme. Gene. 1987;52(2-3):185–195. doi: 10.1016/0378-1119(87)90045-x. [DOI] [PubMed] [Google Scholar]
  2. Appleyard R K. Segregation of New Lysogenic Types during Growth of a Doubly Lysogenic Strain Derived from Escherichia Coli K12. Genetics. 1954 Jul;39(4):440–452. doi: 10.1093/genetics/39.4.440. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bagdasarian M. M., Amann E., Lurz R., Rückert B., Bagdasarian M. Activity of the hybrid trp-lac (tac) promoter of Escherichia coli in Pseudomonas putida. Construction of broad-host-range, controlled-expression vectors. Gene. 1983 Dec;26(2-3):273–282. doi: 10.1016/0378-1119(83)90197-x. [DOI] [PubMed] [Google Scholar]
  4. Brown J. L., Brown D. M., Zabin I. Thiogalactoside transacetylase. Physical and chemical studies of subunit structure. J Biol Chem. 1967 Sep 25;242(18):4254–4258. [PubMed] [Google Scholar]
  5. Deretic V., Gill J. F., Chakrabarty A. M. Gene algD coding for GDPmannose dehydrogenase is transcriptionally activated in mucoid Pseudomonas aeruginosa. J Bacteriol. 1987 Jan;169(1):351–358. doi: 10.1128/jb.169.1.351-358.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. 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]
  7. Débarbouillé M., Raibaud O. Expression of the Escherichia coli malPQ operon remains unaffected after drastic alteration of its promoter. J Bacteriol. 1983 Mar;153(3):1221–1227. doi: 10.1128/jb.153.3.1221-1227.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Figurski D. H., Helinski D. R. Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans. Proc Natl Acad Sci U S A. 1979 Apr;76(4):1648–1652. doi: 10.1073/pnas.76.4.1648. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Frantz B., Chakrabarty A. M. Organization and nucleotide sequence determination of a gene cluster involved in 3-chlorocatechol degradation. Proc Natl Acad Sci U S A. 1987 Jul;84(13):4460–4464. doi: 10.1073/pnas.84.13.4460. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Frantz B., Ngai K. L., Chatterjee D. K., Ornston L. N., Chakrabarty A. M. Nucleotide sequence and expression of clcD, a plasmid-borne dienelactone hydrolase gene from Pseudomonas sp. strain B13. J Bacteriol. 1987 Feb;169(2):704–709. doi: 10.1128/jb.169.2.704-709.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Ghosal D., You I. S., Chatterjee D. K., Chakrabarty A. M. Microbial degradation of halogenated compounds. Science. 1985 Apr 12;228(4696):135–142. doi: 10.1126/science.228.4696.135. [DOI] [PubMed] [Google Scholar]
  12. Goldman A., Ollis D. L., Steitz T. A. Crystal structure of muconate lactonizing enzyme at 3 A resolution. J Mol Biol. 1987 Mar 5;194(1):143–153. doi: 10.1016/0022-2836(87)90723-6. [DOI] [PubMed] [Google Scholar]
  13. Inouye S., Asai Y., Nakazawa A., Nakazawa T. Nucleotide sequence of a DNA segment promoting transcription in Pseudomonas putida. J Bacteriol. 1986 Jun;166(3):739–745. doi: 10.1128/jb.166.3.739-745.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Inouye S., Ebina Y., Nakazawa A., Nakazawa T. Nucleotide sequence surrounding transcription initiation site of xylABC operon on TOL plasmid of Pseudomonas putida. Proc Natl Acad Sci U S A. 1984 Mar;81(6):1688–1691. doi: 10.1073/pnas.81.6.1688. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Inouye S., Nakazawa A., Nakazawa T. Determination of the transcription initiation site and identification of the protein product of the regulatory gene xylR for xyl operons on the TOL plasmid. J Bacteriol. 1985 Sep;163(3):863–869. doi: 10.1128/jb.163.3.863-869.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Inouye S., Nakazawa A., Nakazawa T. Molecular cloning of regulatory gene xylR and operator-promoter regions of the xylABC and xylDEGF operons of the TOL plasmid. J Bacteriol. 1983 Sep;155(3):1192–1199. doi: 10.1128/jb.155.3.1192-1199.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Inouye S., Nakazawa A., Nakazawa T. Nucleotide sequence of the promoter region of the xylDEGF operon on TOL plasmid of Pseudomonas putida. Gene. 1984 Sep;29(3):323–330. doi: 10.1016/0378-1119(84)90061-1. [DOI] [PubMed] [Google Scholar]
  18. Meagher R. B., McCorkle G. M., Ornston M. K., Ornston L. N. Inducible uptake system for -carboxy-cis, cis-muconate in a permeability mutant of Pseudomonas putida. J Bacteriol. 1972 Aug;111(2):465–473. doi: 10.1128/jb.111.2.465-473.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Meagher R. B., Ornston L. N. Relationships among enzymes of the beta-ketoadipate pathway. I. Properties of cis,cis-muconate-lactonizing enzyme and muconolactone isomerase from Pseudomonas putida. Biochemistry. 1973 Aug 28;12(18):3523–3530. doi: 10.1021/bi00742a027. [DOI] [PubMed] [Google Scholar]
  20. Meagher R. B. Purification and partial amino acid sequence of the cyanogen bromide fragments of muconolactone isomerase from Pseudomonas putida. Biochim Biophys Acta. 1977 Sep 27;494(1):33–47. doi: 10.1016/0005-2795(77)90132-5. [DOI] [PubMed] [Google Scholar]
  21. Mermod N., Lehrbach P. R., Reineke W., Timmis K. N. Transcription of the TOL plasmid toluate catabolic pathway operon of Pseudomonas putida is determined by a pair of co-ordinately and positively regulated overlapping promoters. EMBO J. 1984 Nov;3(11):2461–2466. doi: 10.1002/j.1460-2075.1984.tb02156.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Messing J., Crea R., Seeburg P. H. A system for shotgun DNA sequencing. Nucleic Acids Res. 1981 Jan 24;9(2):309–321. doi: 10.1093/nar/9.2.309. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Morse D. E., Baker R. F., Yanofsky C. Translation of the tryptophan messenger RNA of Escherichia coli. Proc Natl Acad Sci U S A. 1968 Aug;60(4):1428–1435. doi: 10.1073/pnas.60.4.1428. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Morse D. E., Yanofsky C. The internal low-efficiency promoter of the tryptophan operon of Escherichia coli. J Mol Biol. 1968 Dec;38(3):447–451. doi: 10.1016/0022-2836(68)90401-4. [DOI] [PubMed] [Google Scholar]
  25. Norrander J., Kempe T., Messing J. Construction of improved M13 vectors using oligodeoxynucleotide-directed mutagenesis. Gene. 1983 Dec;26(1):101–106. doi: 10.1016/0378-1119(83)90040-9. [DOI] [PubMed] [Google Scholar]
  26. Raibaud O., Schwartz M. Positive control of transcription initiation in bacteria. Annu Rev Genet. 1984;18:173–206. doi: 10.1146/annurev.ge.18.120184.001133. [DOI] [PubMed] [Google Scholar]
  27. Schell M. A. Homology between nucleotide sequences of promoter regions of nah and sal operons of NAH7 plasmid of Pseudomonas putida. Proc Natl Acad Sci U S A. 1986 Jan;83(2):369–373. doi: 10.1073/pnas.83.2.369. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Shanley M. S., Neidle E. L., Parales R. E., Ornston L. N. Cloning and expression of Acinetobacter calcoaceticus catBCDE genes in Pseudomonas putida and Escherichia coli. J Bacteriol. 1986 Feb;165(2):557–563. doi: 10.1128/jb.165.2.557-563.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Shine J., Dalgarno L. Determinant of cistron specificity in bacterial ribosomes. Nature. 1975 Mar 6;254(5495):34–38. doi: 10.1038/254034a0. [DOI] [PubMed] [Google Scholar]
  30. Wheelis M. L., Ornston L. N. Genetic control of enzyme induction in the -ketoadipate pathway of Pseudomonas putida: deletion mapping of cat mutations. J Bacteriol. 1972 Feb;109(2):790–795. doi: 10.1128/jb.109.2.790-795.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Wheelis M. L., Stanier R. Y. The genetic control of dissimilatory pathways in Pseudomonas putida. Genetics. 1970 Oct;66(2):245–266. doi: 10.1093/genetics/66.2.245. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Wilson D. B., Hogness D. S. The enzymes of the galactose operon in Escherichia coli. IV. The frequencies of translation of the terminal cistrons in the operon. J Biol Chem. 1969 Apr 25;244(8):2143–2148. [PubMed] [Google Scholar]
  33. Wu C. H., Ornston M. K., Ornston L. N. Genetic control of enzyme induction in the -ketoadipate pathway of Pseudomonas putida: two-point crosses with a regulatory mutant strain. J Bacteriol. 1972 Feb;109(2):796–802. doi: 10.1128/jb.109.2.796-802.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]

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