Structural and functional diversity within the cystatin gene family of Hordeum vulgare

Abraham, Zamira and Martinez Muñoz, Manuel and Carbonero Zalduegui, Pilar and Diaz Rodriguez, Isabel (2006). Structural and functional diversity within the cystatin gene family of Hordeum vulgare. "Journal of Experimental Botany", v. 57 (n. 15); pp. 4245-4255. ISSN 0022-0957. https://doi.org/10.1093/jxb/erl200.

Description

Title: Structural and functional diversity within the cystatin gene family of Hordeum vulgare
Author/s:
  • Abraham, Zamira
  • Martinez Muñoz, Manuel
  • Carbonero Zalduegui, Pilar
  • Diaz Rodriguez, Isabel
Item Type: Article
Título de Revista/Publicación: Journal of Experimental Botany
Date: December 2006
Volume: 57
Subjects:
Faculty: E.T.S. de Ingeniería Agronómica, Alimentaria y de Biosistemas (UPM)
Department: Biotecnología - Biología Vegetal
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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Abstract

Phytocystatins are inhibitors of cysteine proteinases from plants putatively involved in defence and as endogenous regulators of protein turnover. Seven genes encoding cystatins (HvCPI-1 to HvCPI-7), identi-fied from EST collections and from an endosperm cDNA library, have been characterized. The intron–exon structure of their corresponding ORFs has been de-termined and the predicted three-dimensional models for the seven barley cystatins have been established, based on the known crystal structure of oryzacystatin I from rice. Only one out of the seven deduced proteins, HvCPI-7, had sequence variations affecting the three conserved motifs implicated in the enzyme–inhibitor interaction. In three cases, HvCPI-5, HvCPI-6, and HvCPI-7, amino acid differences lead to the prediction of important structural changes in their three-dimensional structures. Northern blot analysis indicated that the seven genes have different expression patterns in barley tissues. The recombinant proteins expressed in Escherichia coli showed distinct inhibitory properties in vitro, with different Ki values, against the three cysteine proteinases tested: papain, cathepsin B, and cathepsin H. Moreover, these recombinant proteins presented dif-ferential fungicidal characteristics inhibiting the growth of phytopathogenic fungi Botrytis cinerea and Fusarium oxysporum in vitro. The resulting implications for the structural and functional diversity of the seven barley cystatins studied are discussed.

Funding Projects

TypeCodeAcronymLeaderTitle
Government of SpainBFU2005-00603UnspecifiedIsabel DíazFunción endógena de una familia de inhibidores de cistein proteasas de cebada

More information

Item ID: 53846
DC Identifier: http://oa.upm.es/53846/
OAI Identifier: oai:oa.upm.es:53846
DOI: 10.1093/jxb/erl200
Official URL: https://academic.oup.com/jxb/article/57/15/4245/551629
Deposited by: Biblioteca ETSI Agrónomos
Deposited on: 04 Feb 2019 14:12
Last Modified: 04 Feb 2019 14:12
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