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. 1986 Mar;165(3):937–941. doi: 10.1128/jb.165.3.937-941.1986

Isolation of Erwinia chrysanthemi kduD mutants altered in pectin degradation.

G Condemine, N Hugouvieux-Cotte-Pattat, J Robert-Baudouy
PMCID: PMC214519  PMID: 3949717

Abstract

Mutants of Erwinia chrysanthemi impaired in pectin degradation were isolated by chemical and Mu d(Ap lac) insertion mutagenesis. A mutation in the kduD gene coding for 2-keto-3-deoxygluconate oxidoreductase prevented the growth of the bacteria on polygalacturonate as the sole carbon source. Analysis of the kduD::Mu d(Ap lac) insertions indicated that kduD is either an isolated gene or the last gene of a polycistronic operon. Some of the Mu d(Ap lac) insertions were kduD-lac fusions in which beta-galactosidase synthesis reflected kduD gene expression. In all these fusions, beta-galactosidase activity was shown to be sensitive to catabolite repression by glucose and to be inducible by polygalacturonate, galacturonate, and other intermediates of polygalacturonate catabolism. Galacturonate-mediated induction was prevented by a mutation which blocked its metabolism to 2-keto-3-deoxygluconate. 2-Keto-3-deoxygluconate appeared to be the true inducer of kduD expression resulting from galacturonate degradation. 5-Keto-4-deoxyuronate or 2,5-diketo-3-deoxygluconate were the true inducers, originating from polygalacturonate cleavage. These three intermediates also appeared to induce pectate lyases, oligogalacturonate lyase, and 5-keto-4-deoxyuronate isomerase synthesis.

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Selected References

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  1. Andro T., Chambost J. P., Kotoujansky A., Cattaneo J., Bertheau Y., Barras F., Van Gijsegem F., Coleno A. Mutants of Erwinia chrysanthemi defective in secretion of pectinase and cellulase. J Bacteriol. 1984 Dec;160(3):1199–1203. doi: 10.1128/jb.160.3.1199-1203.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bertheau Y., Madgidi-Hervan E., Kotoujansky A., Nguyen-The C., Andro T., Coleno A. Detection of depolymerase isoenzymes after electrophoresis or electrofocusing, or in titration curves. Anal Biochem. 1984 Jun;139(2):383–389. doi: 10.1016/0003-2697(84)90022-8. [DOI] [PubMed] [Google Scholar]
  3. Casadaban M. J., Cohen S. N. Lactose genes fused to exogenous promoters in one step using a Mu-lac bacteriophage: in vivo probe for transcriptional control sequences. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4530–4533. doi: 10.1073/pnas.76.9.4530. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Chatterjee A. K., Starr M. P. Genetics of Erwinia species. Annu Rev Microbiol. 1980;34:645–676. doi: 10.1146/annurev.mi.34.100180.003241. [DOI] [PubMed] [Google Scholar]
  5. Chatterjee A. K., Thurn K. K., Tyrell D. J. Isolation and characterization of Tn5 insertion mutants of Erwinia chrysanthemi that are deficient in polygalacturonate catabolic enzymes oligogalacturonate lyase and 3-deoxy-D-glycero-2,5-hexodiulosonate dehydrogenase. J Bacteriol. 1985 May;162(2):708–714. doi: 10.1128/jb.162.2.708-714.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Collmer A., Bateman D. F. Impaired induction and self-catabolite repression of extracellular pectate lyase in Erwinia chrysanthemi mutants deficient in oligogalacturonide lyase. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3920–3924. doi: 10.1073/pnas.78.6.3920. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hugouvieux-Cotte-Pattat N., Quesneau Y., Robert-Baudouy J. Aldohexuronate transport system in Erwinia carotovora. J Bacteriol. 1983 May;154(2):663–668. doi: 10.1128/jb.154.2.663-668.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hugouvieux-Cotte-Pattat N., Robert-Baudouy J. Lactose metabolism in Erwinia chrysanthemi. J Bacteriol. 1985 Apr;162(1):248–255. doi: 10.1128/jb.162.1.248-255.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. KILGORE W. W., STARR M. P. Catabolism of galacturonic and glucuronic acids by Erwinia carotovora. J Biol Chem. 1959 Sep;234:2227–2235. [PubMed] [Google Scholar]
  10. Kotoujansky A., Lemattre M., Boistard P. Utilization of a thermosensitive episome bearing transposon TN10 to isolate Hfr donor strains of Erwinia carotovora subsp. chrysanthemi. J Bacteriol. 1982 Apr;150(1):122–131. doi: 10.1128/jb.150.1.122-131.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Lagarde A. E., Pouysségur J. M., Stoeber F. R. A transport system for 2-keto-3-deoxy-D-gluconate uptake in Escherichia coli K12. Biochemical and physiological studies in whole cells. Eur J Biochem. 1973 Jul 16;36(2):328–341. doi: 10.1111/j.1432-1033.1973.tb02917.x. [DOI] [PubMed] [Google Scholar]
  12. Moran F., Nasuno S., Starr M. P. Extracellular and intracellular polygllacturonic acid trans-eliminases of Erwinia carotovora. Arch Biochem Biophys. 1968 Feb;123(2):298–306. doi: 10.1016/0003-9861(68)90138-0. [DOI] [PubMed] [Google Scholar]
  13. Moran F., Nasuno S., Starr M. P. Oligogalacturonide trans-eliminase of Erwinia carotovora. Arch Biochem Biophys. 1968 Jun;125(3):734–741. doi: 10.1016/0003-9861(68)90508-0. [DOI] [PubMed] [Google Scholar]
  14. PREISS J., ASHWELL G. Polygalacturonic acid metabolism in bacteria. II. Formation and metabolism of 3-deoxy-D-glycero-2, 5-hexodiulosonic acid. J Biol Chem. 1963 May;238:1577–1583. [PubMed] [Google Scholar]
  15. Tsuyumu S. "Self-catabolite repression" of pectate lyase in Erwinia carotovora. J Bacteriol. 1979 Feb;137(2):1035–1036. doi: 10.1128/jb.137.2.1035-1036.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Van Gijsegem F., Toussaint A. In vivo cloning of Erwinia carotovora genes involved in the catabolism of hexuronates. J Bacteriol. 1983 Jun;154(3):1227–1235. doi: 10.1128/jb.154.3.1227-1235.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. van Gijsegem F., Hugouvieux-Cotte-Pattat N., Robert-Baudouy J. Isolation and characterization of Erwinia chrysanthemi mutants defective in degradation of hexuronates. J Bacteriol. 1985 Feb;161(2):702–708. doi: 10.1128/jb.161.2.702-708.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]

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