Isolation and Characterization of the Genes Encoding Basic and Acidic Chitinase in Arabidopsis thaliana
Open Access
- 1 July 1990
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 93 (3), 907-914
- https://doi.org/10.1104/pp.93.3.907
Abstract
Plants synthesize a number of antimicrobial proteins in response to pathogen invasion and environmental stresses. These proteins include two classes of chitinases that have either basic or acidic isoelectric points and that are capable of degrading fungal cell wall chitin. We have cloned and determined the nucleotide sequence of the genes encoding the acidic and basic chitinases from Arabidopsis thaliana (L.) Heynh. Columbia wild type. Both chitinases are encoded by single copy genes that contain introns, a novel feature in chitinase genes. The basic chitinase has 73% amino acid sequence similarity to the basic chitinase from tobacco, and the acidic chitinase has 60% amino acid sequence similarity to the acidic chitinase from cucumber. Expression of the basic chitinase is organ-specific and age-dependent in Arabidopsis. A high constitutive level of expression was observed in roots with lower levels in leaves and flowering shoots. Exposure of plants to ethylene induced high levels of systemic expression of basic chitinase with expression increasing with plant age. Constitutive expression of basic chitinase was observed in roots of the ethylene insensitive mutant (etr) of Arabidopsis, demonstrating that root-specific expression is ethylene independent. Expression of the acidic chitinase gene was not observed in normal, untreated Arabidopsis plants or in plants treated with ethylene or salicylate. However, a transient expression assay indicated that the acidic chitinase promoter is active in Arabidopsis leaf tissue.Keywords
This publication has 24 references indexed in Scilit:
- Functional analysis of DNA sequences responsible for ethylene regulation of a bean chitinase gene in transgenic tobacco.Plant Cell, 1989
- Antifungal Hydrolases in Pea TissuePlant Physiology, 1988
- Pharmacokinetics and adverse effects of amphotericin B in infants and childrenThe Journal of Pediatrics, 1988
- Antifungal Hydrolases in Pea TissuePlant Physiology, 1988
- Several “pathogenesis-related” proteins in potato are 1,3-β-glucanases and chitinasesProceedings of the National Academy of Sciences, 1988
- Primary structure of an endochitinase mRNA fromSolanum tuberosumNucleic Acids Research, 1988
- Cloning of an Arabidopsis thaliana gene encoding 5-enolpyruvylshikimate-3-phosphate synthase: sequence analysis and manipulation to obtain glyphosate-tolerant plantsMolecular Genetics and Genomics, 1987
- Organization and differential activation of a gene family encoding the plant defense enzyme chalcone synthase in Phaseolus vulgarisMolecular Genetics and Genomics, 1987
- [19] Rapid and efficient site-specific mutagenesis without phenotypic selectionMethods in Enzymology, 1987
- Cell Wall Chemistry, Morphogenesis, and Taxonomy of FungiAnnual Review of Microbiology, 1968