Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Plant Physiology 91:119-123 (1989)
© 1989 American Society of Plant Biologists

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Vera, P.
Right arrow Articles by Conejero, V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Vera, P.
Right arrow Articles by Conejero, V.
Agricola
Right arrow Articles by Vera, P.
Right arrow Articles by Conejero, V.
Microbe-Plant Interactions

Immunogold Localization of the Citrus Exocortis Viroid-Induced Pathogenesis-Related Proteinase P69 in Tomato Leaves 1

Pablo Vera, José Hernández Yago and Vicente Conejero

Departamento de Biotecnología, Universidad Politécnica de Valencia, 46022-Valencia, Spain, Instituto de Investigaciones Citológicas, 46010-Valencia, Spain

Citrus exocortis viroid induces in tomato plants (Lycopersicon esculentum) synthesis and accumulation of a pathogenesis-related protein (P69) previously reported to be a proteinase (Vera P, Conejero V [1988] Plant Physiol 87: 58-63). By immunogold/transmission electron microscopy, we have studied the distribution of this protein in thin sections of parenchymatous leaf tissue. The enzyme was present intra- and extracellularly. The intracellular location was limited to the vacuole and was always associated with engulfed cell material. When extracellularly located, the enzyme was associated with a dispersed, electron-dense material in the intercellular spaces. This latter location was confirmed after analysis of intercellular washing fluids obtained by vacuum infiltration of leaves. These observations provide new data for the understanding of viroid pathogenesis and the biological role of the pathogenesis-related proteinase P69.


1 This research was supported in part by grants from CAICYT (2509/84) and from Diputación de Valencia, Spain.




This article has been cited by other articles:


Home page
Crop Sci.Home page
N. S. Nelsen, Z. Li, A. L. Warner, B. F. Matthews, and H. T. Knap
Genomic Polymorphism Identifies a Subtilisin-Like Protease near the Rhg4 Locus in Soybean
Crop Sci., January 1, 2004; 44(1): 265 - 273.
[Abstract] [Full Text] [PDF]


Home page
Genes Dev.Home page
D. Berger and T. Altmann
A subtilisin-like serine protease involved in the regulation of stomatal density and distribution in Arabidopsis thaliana
Genes & Dev., May 1, 2000; 14(9): 1119 - 1131.
[Abstract] [Full Text]


Home page
J. Biol. Chem.Home page
L. Jorda, A. Coego, V. Conejero, and P. Vera
A Genomic Cluster Containing Four Differentially Regulated Subtilisin-like Processing Protease Genes Is in Tomato Plants
J. Biol. Chem., January 22, 1999; 274(4): 2360 - 2365.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
P. Tornero, V. Conejero, and P. Vera
Identification of a New Pathogen-induced Member of the Subtilisin-like Processing Protease Family from Plants
J. Biol. Chem., May 30, 1997; 272(22): 14412 - 14419.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1989 by the American Society of Plant Biologists