Skip to main content

Some NLM-NCBI services and products are experiencing heavy traffic, which may affect performance and availability. We apologize for the inconvenience and appreciate your patience. For assistance, please contact our Help Desk at info@ncbi.nlm.nih.gov.

Journal of Bacteriology logoLink to Journal of Bacteriology
. 1968 Nov;96(5):1488–1499. doi: 10.1128/jb.96.5.1488-1499.1968

Genetic Control of the β-Ketoadipate Pathway in Pseudomonas aeruginosa

M B Kemp a,1, G D Hegeman a
PMCID: PMC315200  PMID: 4973125

Abstract

The regulation and genetic control of the β-ketoadipate pathway in Pseudomonas aeruginosa were investigated. The pattern of enzyme induction is apparently the same as in P. putida. Mutants were obtained for all but 1 of the 11 structural genes; the proximity of these genes on the chromosome was examined by transduction of the mutants with phage F116. If a group of enzymes was induced by the same compounds, the corresponding genes were closely clustered. Surprisingly, some locispecifying enzymes not sharing a common inducer were also clustered. It is suggested that this latter finding may indicate a degree of chromosomal specialization.

Full text

PDF
1488

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. AMES B. N., MARTIN R. G. BIOCHEMICAL ASPECTS OF GENETICS: THE OPERON. Annu Rev Biochem. 1964;33:235–258. doi: 10.1146/annurev.bi.33.070164.001315. [DOI] [PubMed] [Google Scholar]
  2. BURTON J. F., CAIN B. F. Antileukaemic activity of polyporic acid. Nature. 1959 Oct 24;184(Suppl 17):1326–1327. doi: 10.1038/1841326a0. [DOI] [PubMed] [Google Scholar]
  3. Baumann P., Doudoroff M., Stanier R. Y. A study of the Moraxella group. II. Oxidative-negative species (genus Acinetobacter). J Bacteriol. 1968 May;95(5):1520–1541. doi: 10.1128/jb.95.5.1520-1541.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Brammar W. J., Clarke P. H., Skinner A. J. Biochemical and genetic studies with regulator mutants of the Pseudomonas aeruginosa 8602 amidase system. J Gen Microbiol. 1967 Apr;47(1):87–102. doi: 10.1099/00221287-47-1-87. [DOI] [PubMed] [Google Scholar]
  5. CLOWES R. C. Investigation of the genetics of cysteineless mutants of Salmonella typhimurium by transduction. J Gen Microbiol. 1958 Feb;18(1):154–172. doi: 10.1099/00221287-18-1-154. [DOI] [PubMed] [Google Scholar]
  6. Chakrabarty A. M., Gunsalus C. F., Gunsalus I. C. Transduction and the clustering of genes in fluorescent Pseudomonads. Proc Natl Acad Sci U S A. 1968 May;60(1):168–175. doi: 10.1073/pnas.60.1.168. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Crawford I. P., Gunsalus I. C. Inducibility of tryptophan synthetase in Pseudomonas putida. Proc Natl Acad Sci U S A. 1966 Aug;56(2):717–724. doi: 10.1073/pnas.56.2.717. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Cánovas J. L., Stanier R. Y. Regulation of the enzymes of the beta-ketoadipate pathway in Moraxella calcoacetica. 1. General aspects. Eur J Biochem. 1967 May;1(3):289–300. doi: 10.1007/978-3-662-25813-2_40. [DOI] [PubMed] [Google Scholar]
  9. Cánovas J. L., Wheelis M. L., Stanier R. Y. Regulation of the enzymes of the beta-ketoadipate pathway in Moraxella calcoacetica. 2. The role of protocatechuate as inducer. Eur J Biochem. 1968 Jan;3(3):293–304. doi: 10.1111/j.1432-1033.1968.tb19529.x. [DOI] [PubMed] [Google Scholar]
  10. DEMEREC M. CLUSTERING OF FUNCTIONALLY RELATED GENES IN SALMONELLA TYPHIMURIUM. Proc Natl Acad Sci U S A. 1964 Jun;51:1057–1060. doi: 10.1073/pnas.51.6.1057. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Demerec M., Adelberg E. A., Clark A. J., Hartman P. E. A proposal for a uniform nomenclature in bacterial genetics. Genetics. 1966 Jul;54(1):61–76. doi: 10.1093/genetics/54.1.61. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Evans W. C. Oxidation of phenol and benzoic acid by some soil bacteria. Biochem J. 1947;41(3):373–382. doi: 10.1042/bj0410373. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. FARGIE B., HOLLOWAY B. W. ABSENCE OF CLUSTERING OF FUNCTIONALLY RELATED GENES IN PSEUDOMONAS AERUGINOSA. Genet Res. 1965 Jul;6:284–299. doi: 10.1017/s0016672300004158. [DOI] [PubMed] [Google Scholar]
  14. HOLLOWAY B. W., EGAN J. B., MONK M. Lysogeny in Pseudomonas aeruginosa. Aust J Exp Biol Med Sci. 1960 Aug;38:321–329. doi: 10.1038/icb.1960.34. [DOI] [PubMed] [Google Scholar]
  15. HOLLOWAY B. W. Genetic recombination in Pseudomonas aeruginosa. J Gen Microbiol. 1955 Dec;13(3):572–581. doi: 10.1099/00221287-13-3-572. [DOI] [PubMed] [Google Scholar]
  16. Hegeman G. D. Synthesis of the enzymes of the mandelate pathway by Pseudomonas putida. I. Synthesis of enzymes by the wild type. J Bacteriol. 1966 Mar;91(3):1140–1154. doi: 10.1128/jb.91.3.1140-1154.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Hosokawa K., Stanier R. Y. Crystallization and properties of p-hydroxybenzoate hydroxylase from Pseudomonas putida. J Biol Chem. 1966 May 25;241(10):2453–2460. [PubMed] [Google Scholar]
  18. JACOB F., MONOD J. Genetic regulatory mechanisms in the synthesis of proteins. J Mol Biol. 1961 Jun;3:318–356. doi: 10.1016/s0022-2836(61)80072-7. [DOI] [PubMed] [Google Scholar]
  19. LOUTIT J. S. A transduction-like process within a single strain of Pseudomonas aeruginosa. J Gen Microbiol. 1958 Apr;18(2):315–319. doi: 10.1099/00221287-18-2-315. [DOI] [PubMed] [Google Scholar]
  20. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  21. Mee B. J., Lee B. T. An analysis of histidine requiring mutants in Pseudomonas aeruginosa. Genetics. 1967 Apr;55(4):709–722. doi: 10.1093/genetics/55.4.709. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Ornston L. N., Stanier R. Y. The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida. J Biol Chem. 1966 Aug 25;241(16):3776–3786. [PubMed] [Google Scholar]
  23. Ornston L. N. The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida. 3. Enzymes of the catechol pathway. J Biol Chem. 1966 Aug 25;241(16):3795–3799. [PubMed] [Google Scholar]
  24. Ornston L. N. The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida. II. Enzymes of the protocatechuate pathway. J Biol Chem. 1966 Aug 25;241(16):3787–3794. [PubMed] [Google Scholar]
  25. Ornston L. N. The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida. IV. Regulation. J Biol Chem. 1966 Aug 25;241(16):3800–3810. [PubMed] [Google Scholar]
  26. PEARCE L. E., LOUTIT J. S. BIOCHEMICAL AND GENETIC GROUPING OF ISOLEUCINE-VALINE MUTANTS OF PSEUDOMONAS AERUGINOSA. J Bacteriol. 1965 Jan;89:58–63. doi: 10.1128/jb.89.1.58-63.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. STANIER R. Y., INGRAHAM J. L. Protocatechuic acid oxidase. J Biol Chem. 1954 Oct;210(2):799–808. [PubMed] [Google Scholar]
  28. Stanier R. Y., Palleroni N. J., Doudoroff M. The aerobic pseudomonads: a taxonomic study. J Gen Microbiol. 1966 May;43(2):159–271. doi: 10.1099/00221287-43-2-159. [DOI] [PubMed] [Google Scholar]
  29. Stanier R. Y. Simultaneous Adaptation: A New Technique for the Study of Metabolic Pathways. J Bacteriol. 1947 Sep;54(3):339–348. doi: 10.1128/jb.54.3.339-348.1947. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Taylor A. L., Trotter C. D. Revised linkage map of Escherichia coli. Bacteriol Rev. 1967 Dec;31(4):332–353. doi: 10.1128/br.31.4.332-353.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES