Abstract
An antiserum raised against a purified tobacco beta-1,3-glucanase (PR-N) was used to study the subcellular localization of enzyme in fungus-infected plant tissues by means of post-embedding immunogold labeling. In susceptible tomato plants, the enzyme accumulation was found to occur as a result of successful tissue colonization, whereas it appeared to be an early event associated with limited spread of the fungus in resistant tissues. Although marked differences between susceptible and resistant tomato cultivars were observed in the rate of production of beta-1,3-glucanase, the pattern of enzyme distribution was similar. The enzyme was found to accumulate predominantly in host cell walls and secondary thickenings of xylem vessels. By contrast, a very low amount of enzyme was associated with compound middle lamellae. The occurrence of beta-1,3-glucanase at the cell surface of invading fungi was an indication of their possible antifungal activity. A low enzyme concentration was detected in vacuoles of both healthy and infected tissues. In infected eggplant tissue, the pattern of beta-1,3-glucanase distribution was similar to that observed with tomato. Whether these hydrolases accumulate first in vacuoles and are subsequently conveyed toward the outside to participate in fungal wall lysis remains to be determined.
Full Text
The Full Text of this article is available as a PDF (4.9 MB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Bulcke M. V., Bauw G., Castresana C., Van Montagu M., Vandekerckhove J. Characterization of vacuolar and extracellular beta(1,3)-glucanases of tobacco: Evidence for a strictly compartmentalized plant defense system. Proc Natl Acad Sci U S A. 1989 Apr;86(8):2673–2677. doi: 10.1073/pnas.86.8.2673. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Côté F., Letarte J., Grenier J., Trudel J., Asselin A. Detection of beta-1,3-glucanase activity after native polyacrylamide gel electrophoresis: application to tobacco pathogenesis-related proteins. Electrophoresis. 1989 Jul;10(7):527–529. doi: 10.1002/elps.1150100714. [DOI] [PubMed] [Google Scholar]
- Joosten M. H., De Wit P. J. Identification of Several Pathogenesis-Related Proteins in Tomato Leaves Inoculated with Cladosporium fulvum (syn. Fulvia fulva) as 1,3-beta-Glucanases and Chitinases. Plant Physiol. 1989 Mar;89(3):945–951. doi: 10.1104/pp.89.3.945. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Keen N. T., Yoshikawa M. beta-1,3-Endoglucanase from Soybean Releases Elicitor-Active Carbohydrates from Fungus Cell Walls. Plant Physiol. 1983 Mar;71(3):460–465. doi: 10.1104/pp.71.3.460. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kombrink E., Schröder M., Hahlbrock K. Several "pathogenesis-related" proteins in potato are 1,3-beta-glucanases and chitinases. Proc Natl Acad Sci U S A. 1988 Feb;85(3):782–786. doi: 10.1073/pnas.85.3.782. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Legrand M., Kauffmann S., Geoffroy P., Fritig B. Biological function of pathogenesis-related proteins: Four tobacco pathogenesis-related proteins are chitinases. Proc Natl Acad Sci U S A. 1987 Oct;84(19):6750–6754. doi: 10.1073/pnas.84.19.6750. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mauch F., Hadwiger L. A., Boller T. Antifungal Hydrolases in Pea Tissue : I. Purification and Characterization of Two Chitinases and Two beta-1,3-Glucanases Differentially Regulated during Development and in Response to Fungal Infection. Plant Physiol. 1988 Jun;87(2):325–333. doi: 10.1104/pp.87.2.325. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]