Skip to main content

Identification and expression studies of a catalase and a bifunctional catalase-peroxidase in Frankia strain R43

  • Conference paper
Frankia Symbiosis

Part of the book series: Developments in Plant and Soil Sciences ((DPSS,volume 100))

  • 164 Accesses

Abstract

A rnonofunctional catalase and a bifunctional catalase-peroxidase were revealed by activity staining of nondenaturing PAGE in Frankia strain R43. Both enzymes were shown to be cytoplasmatic, growth regulated and expressed mainly during the stationary growth phase. Nevertheless, low levels of constitutive expression could also be detected during the early stages of growth. Immunoblot analyses using a polyclonal antibody raised against a catalase-peroxidase purified from Streptomyces reticuli showed a band of 83.2 kDa, with the same growth dependent pattern as obtained by the nondenaturing PAGE analyses. Induction studies revealed that both enzymes were strongly induced by raising the intracellular concentration of H2O2 with paraquat, but not with exogenous H2O2. In addition, no acquisition of tolerance to exogenous H2O2 was observed whatever the pretreatment of the inocula, i.e. despite the expression level of both hydroperoxidases.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 169.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 219.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 219.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Alskog G and Huss-Danell K 1997 Superoxide dismutase, catalase and nitrogenase activities of symbiotic Frankia (Alnus incana) in response to different oxygen tensions. Physiol. Plant. 99, 286–292.

    Article  CAS  Google Scholar 

  • Brown S M, Howell M L, Vasil M L, Anderson A J and Has-sett D J 1995 Cloning and characterization of the katB gene of Pseudomonas aeruginosa encoding a hydrogen peroxide-inducible catalase: purification of katB, cellular localization, and demonstration that is essential for optimal resistance to hydrogen peroxide. J. Bacteriol. 177, 6536–6544.

    PubMed  CAS  Google Scholar 

  • Clare D A, Duong M N, Dan D, Archibald F and Fridovich 1984 Effects of molecular oxygen on detection of superoxide radical with nitro blue tetrazolium and on activity stain for catalasc. Anal. Biochem. 140, 532–537.

    Article  PubMed  CAS  Google Scholar 

  • Conyers S M and Kidwell D A 1991 Chromogenic substrates for horseradish peroxidase. Anal. Biochem. 192, 207–211.

    Article  PubMed  CAS  Google Scholar 

  • Dalton D A, Hanus F J, Russel S A and Evans H J 1987 Purification, properties, and distribution of ascorbate peroxidase in legume root nodules. Plant Physiol. 83, 789–794.

    Article  PubMed  CAS  Google Scholar 

  • Dowds B C A 1994 The oxidative stress response in Bacillus subtilis. FEMS Microbiol. Lett. 124, 255–264.

    CAS  Google Scholar 

  • Farr S B and Kogoma T 1991 Oxidative stress responses in Escherichia coli and Salmonella typhimurium. Microbiol. Rev. 55, 561–585.

    PubMed  CAS  Google Scholar 

  • Fontaine M S, Young P H and Torrey J G 1986 Effects of longterm preservation of Frankia strains on infectivity, effectivity, and in vitro nitrogenase activity. Appl. Environ. Microbiol. 51, 694–698.

    PubMed  CAS  Google Scholar 

  • Fraaije M W, Rouhroeks H P and Hagen W R 1996 Purification and characterization of an intracellular catalase-peroxidase from Penicillium simplicissimurn. Eur. J. Biochem. 235, 192–198.

    Article  PubMed  CAS  Google Scholar 

  • Green M J and Hill H A O 1984 Chemistry of dioxygen. Methods Enzymol. 105, 3–22.

    Google Scholar 

  • Hérouart D, Sigaud S, Moreau S, Frendo P, Touati D and Puppo A 1996 Cloning and characterization of the katA gene of Rhizobium meliloti encoding a hydrogen peroxide-inducible catalase. J. Bacteriol. 178, 6802–6809.

    PubMed  Google Scholar 

  • Hochman A, Figueredo A and Wall J D 1992 Physiological functions of hydroperoxidases in Rhodobacter capsulatus. J. Bacteriol. 174, 3386–3391.

    PubMed  CAS  Google Scholar 

  • Klotz M G and Hutcheson S W 1992 Multiple periplasmic catalases in phytopathogenic strains of Pseudomonas syringae. Appl. Environ. Microbiol. 58, 2468–2473.

    PubMed  CAS  Google Scholar 

  • Levine A, Tenhaken R, Dixon R and Lamb C 1994 H202 from the oxidative burst orchestrates the plant hypersensitive disease resistance response. Cell 79, 583–593.

    Article  PubMed  CAS  Google Scholar 

  • Levy E, Eyal Z and Hochman A 1992 Purification and characterization of a catalase-peroxidase from the fungus Septoria tritici. Arch. Biochem. Biophys. 296, 321–327.

    Article  PubMed  CAS  Google Scholar 

  • Long S R and Staskawicz B J 1993 Prokaryotic plant parasites. Cell 73, 921–935.

    Article  PubMed  CAS  Google Scholar 

  • Ma M and Eaton J W 1992 Multicellular oxidant defense in unicel- lular organisms. Proc. Natl. Acad. Sci. USA 89, 7924–7928.

    Article  PubMed  CAS  Google Scholar 

  • Nadler V, Goldberg I and Hochman A 1986 Comparative study of bacterial catalases. Bioch. Biophys. Acta 882, 234–241.

    Google Scholar 

  • Puppo A, Dimitrijevic L and Rigaud J 1989 Superoxide dismutase and catalase activities in purified Frankia vesicles. Physiol. Plant. 77, 308–311.

    Article  CAS  Google Scholar 

  • Puppo A, Dimitrijevic L, Diem H G and Dommergues Y R 1985 Homogeneity of superoxide dismutase patterns in Frankia strains from Casuarinaceae. FEMS Microbiol. Lett. 30, 43–46.

    Article  CAS  Google Scholar 

  • Sigaud S, Becquet V, Frendo P, Puppo A and Hérouart D 1999 Differential regulation of two divergent Sinorhizobium meliloti genes for HPII-like catalases during free-living growth and protective role of both catalases during symbiosis. J. Bacteriol. 181, 2634–2639.

    PubMed  CAS  Google Scholar 

  • Steele D B and Stowers M D 1986 Superoxide dismutase and catalase in Frankia. Can. J. Microbiol. 32, 409–413.

    Article  CAS  Google Scholar 

  • Steinman H M, Fareed F and Weinstein L 1997 Catalase-peroxidase of Caulobacter crescentus: Function and role in stationary phase survival. J. Bacteriol. 179, 6831–6836.

    Google Scholar 

  • Tavares F and Sellstedt A 2000 A simple, rapid and non-destructive procedure to extract cell wall-associated proteins from Frankia. J. Microbiol. Meth. 39, 171–178.

    Article  CAS  Google Scholar 

  • Welinder K G 1991 Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily. Biochim. Biophys. Acta 1080, 215–220.

    Google Scholar 

  • Zou P-J, Borovok I, Lucana D O O, Müller D and Schrempf H 1999 The mycelium-associated Streptonrvices reticuli catalaseperoxidase, its gene and regulation by FurS. Microbiology 145. 549–559.

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Fernando Tavares .

Editor information

P. Normand J. O. Dawson K. Pawlowski

Rights and permissions

Reprints and permissions

Copyright information

© 2003 Springer Science+Business Media Dordrecht

About this paper

Cite this paper

Tavares, F., Bernardo, L., Sellstedt, A. (2003). Identification and expression studies of a catalase and a bifunctional catalase-peroxidase in Frankia strain R43. In: Normand, P., Dawson, J.O., Pawlowski, K. (eds) Frankia Symbiosis. Developments in Plant and Soil Sciences, vol 100. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-1601-7_9

Download citation

  • DOI: https://doi.org/10.1007/978-94-017-1601-7_9

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-90-481-6380-9

  • Online ISBN: 978-94-017-1601-7

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics