Abstract
Early plant defense response is characterized by elevation of activity of peroxidases and enhanced insolubilization of hydroxyproline-rich glycoproteins, such as extensin, in the cell wall. The insolubilization process (cross-linking between soluble extensin precursor molecules) is catalyzed by extensin peroxidases. We have ionically eluted extensin peroxidases from intact water-washed suspension-cultured tomato (hybrid of Lycopersicon esculentum Mill. and Lycopersicon peruvianum L. [Mill.]) cells and purified them to homogeneity by molecular sieve and cation-exchange chromatography. Four ionic forms of peroxidase (PI,PII,EPIII, and EPIV) were resolved; only the latter two cross-linked tomato soluble extensin. The molecular weight (34,000-37,000), amino acid composition, and isoelectric point (9.0) of the extensin peroxidases were determined. Substrate specificities of the enzymes were investigated: soluble extensin and potato lectin (a hydroxyproline-rich glycoprotein with a domain that strongly resembles extensin) were cross-linked by only two forms of the enzyme, whereas bovine serum albumin, aldolase, insulin, a number of other marker proteins, and proteins eluted from tomato cells (except extensin) could not be cross-linked. We have also isolated a yeast elicitor that enhances total peroxidase activity and extensin insolubilization within 1 h of challenge in cultured cells of tomato. A highly sensitive enzyme-linked immunosorbent assay technique using polyclonal antiserum raised against soluble tomato extensin was used to demonstrate extensin insolubilization in vivo. A tomato cell-wall peroxidase that cross-links extensin has been purified and may have a role in plant defense.
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Selected References
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- Allen A. K., Desai N. N., Neuberger A., Creeth J. M. Properties of potato lectin and the nature of its glycoprotein linkages. Biochem J. 1978 Jun 1;171(3):665–674. doi: 10.1042/bj1710665. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Allen A. K., Neuberger A. The purification and properties of the lectin from potato tubers, a hydroxyproline-containing glycoprotein. Biochem J. 1973 Oct;135(2):307–314. doi: 10.1042/bj1350307. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Basse C. W., Boller T. Glycopeptide elicitors of stress responses in tomato cells: N-linked glycans are essential for activity but act as suppressors of the same activity when released from the glycopeptides. Plant Physiol. 1992 Apr;98(4):1239–1247. doi: 10.1104/pp.98.4.1239. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
- Bradley D. J., Kjellbom P., Lamb C. J. Elicitor- and wound-induced oxidative cross-linking of a proline-rich plant cell wall protein: a novel, rapid defense response. Cell. 1992 Jul 10;70(1):21–30. doi: 10.1016/0092-8674(92)90530-p. [DOI] [PubMed] [Google Scholar]
- Brownleader M. D., Dey P. M. Purification of extensin from cell walls of tomato (hybrid of Lycopersicon esculentum and L. peruvianum) cells in suspension culture. Planta. 1993;191(4):457–469. doi: 10.1007/BF00195747. [DOI] [PubMed] [Google Scholar]
- Cooper J. B., Varner J. E. Cross-linking of soluble extensin in isolated cell walls. Plant Physiol. 1984 Oct;76(2):414–417. doi: 10.1104/pp.76.2.414. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Esquerré-Tugayé M. T. Cell Surfaces in Plant-Microorganism Interactions: I. A Structural Investigation of Cell Wall Hydroxyproline-rich Glycoproteins Which Accumulate in Fungus-infected Plants. Plant Physiol. 1979 Aug;64(2):314–319. doi: 10.1104/pp.64.2.314. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Esquerré-Tugayé M. T., Lafitte C., Mazau D., Toppan A., Touzé A. Cell Surfaces in Plant-Microorganism Interactions: II. Evidence for the Accumulation of Hydroxyproline-rich Glycoproteins in the Cell Wall of Diseased Plants as a Defense Mechanism. Plant Physiol. 1979 Aug;64(2):320–326. doi: 10.1104/pp.64.2.320. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Everdeen D. S., Kiefer S., Willard J. J., Muldoon E. P., Dey P. M., Li X. B., Lamport D. T. Enzymic cross-linkage of monomeric extensin precursors in vitro. Plant Physiol. 1988 Jul;87(3):616–621. doi: 10.1104/pp.87.3.616. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hahn M. G., Albersheim P. Host-Pathogen Interactions: XIV. Isolation and Partial Characterization of an Elicitor from Yeast Extract. Plant Physiol. 1978 Jul;62(1):107–111. doi: 10.1104/pp.62.1.107. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kerby K., Somerville S. C. Purification of an infection-related, extracellular peroxidase from barley. Plant Physiol. 1992 Sep;100(1):397–402. doi: 10.1104/pp.100.1.397. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- Lamb C. J., Dixon R. A. Molecular mechanisms underlying induction of plant defence gene transcription. Biochem Soc Symp. 1994;60:241–248. [PubMed] [Google Scholar]
- Zimmerlin A., Wojtaszek P., Bolwell G. P. Synthesis of dehydrogenation polymers of ferulic acid with high specificity by a purified cell-wall peroxidase from French bean (Phaseolus vulgaris L.). Biochem J. 1994 May 1;299(Pt 3):747–753. doi: 10.1042/bj2990747. [DOI] [PMC free article] [PubMed] [Google Scholar]