Modulating the proteinase inhibitory profile of a plant cystatin by single mutations at positively selected amino acid sites

Cysteine proteinase inhibitors of the cystatin superfamily have several important functions in plants, including the inhibition of exogenous cysteine proteinases during herbivory or infection. Here we used a maximum-likelihood approach to assess whether plant cystatins, like other proteins implicate...

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Veröffentlicht in:	The Plant journal : for cell and molecular biology Jg. 48; H. 3; S. 403 - 413
Hauptverfasser:	Kiggundu, Andrew, Goulet, Marie-Claire, Goulet, Charles, Dubuc, Jean-François, Rivard, Daniel, Benchabane, Meriem, Pépin, Geneviève, Vyver, Christell van der, Kunert, Karl, Michaud, Dominique
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	Oxford, UK Oxford, UK : Blackwell Publishing Ltd 01.11.2006 Blackwell Publishing Ltd Blackwell Science
Schlagworte:	Agronomy. Soil science and plant productions Amino Acids Amino Acids - chemistry Base Sequence binding properties Binding sites Biological and medical sciences cathepsin B cathepsin H chemistry Codon cystatins Cystatins - chemistry Cystatins - pharmacology Cysteine Proteinase Inhibitors Cysteine Proteinase Inhibitors - pharmacology DNA Primers evolution Flowers & plants functional diversity Fundamental and applied biological sciences. Psychology Genetics and breeding of economic plants Herbivory Likelihood Functions Lycopersicon esculentum Models, Molecular Mutagenesis mutants Mutation papain pharmacology Plant breeding: fundamental aspects and methodology plant cystatins plant–insect interactions Poaceae positive selection Proteinase inhibitors Proteins site-directed mutagenesis Solanaceae Tomatoes Cystatin EC 3.4.22.16 Monocotyledones Cysteine plant cystatins Pest cysteine proteinase inhibitors Gramineae plant-insect interactions Dicotyledones Aminoacid Angiospermae Lycopersicon esculentum site- directed mutagenesis Spermatophyta EC 3.4.22.1 positive selection Inhibition Mutation Solanaceae EC 3.4.22.2
ISSN:	0960-7412, 1365-313X
Online-Zugang:	Volltext
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