http://www.cnr.it/ontology/cnr/individuo/prodotto/ID12863

Identification and characterization of protease inhibitors in Diplotaxis species (Articolo in rivista)

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Identification and characterization of protease inhibitors in Diplotaxis species (Articolo in rivista) (literal)

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Mariateresa Volpicella, Francesca De Leo, Marta Sciancalepore, Gabriella Sonnante, Domenico Pignone, Raffaele Gallerani, Luigi R. Ceci (2009)
Identification and characterization of protease inhibitors in Diplotaxis species
in Plant physiology and biochemistry (Paris); Academic Press Elsevier, Amsterdam (Paesi Bassi)
(literal)

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Mariateresa Volpicella, Francesca De Leo, Marta Sciancalepore, Gabriella Sonnante, Domenico Pignone, Raffaele Gallerani, Luigi R. Ceci (literal)

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a Department of Biochemistry and Molecular Biology, University of Bari, Via Amendola 165/A, 70126 Bari, Italy b Institute for Biomembranes and Bioenergetic, CNR, Via Amendola 165/A, 70126 Bari, Italy c Institute of Plant Genetics, CNR, Via Amendola 165/A, 70126 Bari, Italy (literal)

Titolo

Identification and characterization of protease inhibitors in Diplotaxis species (literal)

Abstract

PCR analysis of the genomes of two wild Brassicaceae plants, Diplotaxis muralis and D. tenuifolia, demonstrated the presence of several genes coding for potential protease inhibitors, classifiable within the Mustard Inhibitor family (MSI). This is a small family of plant protease inhibitors named after the mustard trypsin inhibitor MTI-2, the first protease inhibitor characterised in Brassicaceae. From identified sequences two recombinant inhibitors were expressed in Pichia pastoris. In comparison with MTI-2, they show a reduced activity against bovine trypsin. However, when tested against trypsin-like proteases present in the guts of Helicoverpa zea larvae, the Diplotaxis inhibitors and MTI-2 show similar activities, indicating that the usually adopted procedure of reporting activity of plant protease inhibitors against bovine trypsin may lead to wrong estimation of their effect on insect proteases. This issue is of particular relevance when planning the use of PI genes for developing insect resistant plants. (literal)

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