Leucine aminopeptidase: an inducible component of the defense response in Lycopersicon esculentum (tomato).
- 1 November 1993
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 90 (21) , 9906-9910
- https://doi.org/10.1073/pnas.90.21.9906
Abstract
A leucine aminopeptidase (EC 3.4.11.1) cDNA clone (DR57) that was induced in response to Pseudomonas syringae pv. tomato (P.s. tomato) infection was isolated using a subtractive hybridization-enriched cDNA probe. Genomic DNA blot analysis showed that the tomato genome had two leucine aminopeptidase genes. The levels of DR57 mRNAs after P.s. tomato infection and mechanical wounding were determined in two inbred tomato lines that exhibit susceptibility and resistance to P.s. tomato. DR57 mRNAs were detected 12 hours after infection and 4 hours after wounding. Furthermore, DR57 mRNAs were systemically induced in response to wounding. DR57 mRNAs were induced in leaves after Spodoptera littoralis feeding but were not detected in detached leaf controls. Possible roles for the DR57 leucine aminopeptidase in the defense reactions are discussed.Keywords
This publication has 40 references indexed in Scilit:
- Ethylene Signal Is Transduced via Protein Phosphorylation Events in Plants.Plant Cell, 1993
- General roles of abscisic and jasmonic acids in gene activation as a result of mechanical wounding.Plant Cell, 1992
- Differential Expression of Tomato Proteinase Inhibitor I and II Genes During Bacterial Pathogen Invasion and WoundingMolecular Plant-Microbe Interactions®, 1991
- Increase of Chalcone Synthase mRNA in Pathogen-Inoculated Soybeans with Race-Specific Resistance Is Different in Leaves and RootsPlant Physiology, 1989
- Proteinase inhibitor gene families: Strategies for transformation to improve plant defenses against herbivoresBioEssays, 1989
- Characterization and Subcellular Localization of Aminopeptidases in Senescing Barley LeavesPlant Physiology, 1988
- In Vivo Half-Life of a Protein Is a Function of Its Amino-Terminal ResidueScience, 1986
- Inactivation and Metabolism of NeuropeptidesAnnual Review of Neuroscience, 1986
- Screening λgt Recombinant Clones by Hybridization to Single Plaques in SituScience, 1977
- Wound-Induced Proteinase Inhibitor in Plant Leaves: A Possible Defense Mechanism against InsectsScience, 1972