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HvPap-1 C1A Protease Participates Differentially in the Barley Response to a Pathogen and an Herbivore

Co-evolutionary processes in plant–pathogen/herbivore systems indicate that protease inhibitors have a particular value in biotic interactions. However, little is known about the defensive role of their targets, the plant proteases. C1A cysteine proteases are the most abundant enzymes responsible fo...

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Autores principales: Diaz-Mendoza, Mercedes, Velasco-Arroyo, Blanca, Santamaria, M. Estrella, Diaz, Isabel, Martinez, Manuel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5601043/
https://www.ncbi.nlm.nih.gov/pubmed/28955371
http://dx.doi.org/10.3389/fpls.2017.01585
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author Diaz-Mendoza, Mercedes
Velasco-Arroyo, Blanca
Santamaria, M. Estrella
Diaz, Isabel
Martinez, Manuel
author_facet Diaz-Mendoza, Mercedes
Velasco-Arroyo, Blanca
Santamaria, M. Estrella
Diaz, Isabel
Martinez, Manuel
author_sort Diaz-Mendoza, Mercedes
collection PubMed
description Co-evolutionary processes in plant–pathogen/herbivore systems indicate that protease inhibitors have a particular value in biotic interactions. However, little is known about the defensive role of their targets, the plant proteases. C1A cysteine proteases are the most abundant enzymes responsible for the proteolytic activity during different processes like germination, development and senescence in plants. To identify and characterize C1A cysteine proteases of barley with a potential role in defense, mRNA and protein expression patterns were analyzed in response to biotics stresses. A barley cysteine protease, HvPap-1, previously related to abiotic stresses and grain germination, was particularly induced by flagellin or chitosan elicitation, and biotic stresses such as the phytopathogenic fungus Magnaporthe oryzae or the phytophagous mite Tetranychus urticae. To elucidate the in vivo participation of this enzyme in defense, transformed barley plants overexpressing or silencing HvPap-1 encoding gene were subjected to M. oryzae infection or T. urticae infestation. Whereas overexpressing plants were less susceptible to the fungus than silencing plants, the opposite behavior occurred to the mite. This unexpected result highlights the complexity of the regulatory events leading to the response to a particular biotic stress.
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spelling pubmed-56010432017-09-27 HvPap-1 C1A Protease Participates Differentially in the Barley Response to a Pathogen and an Herbivore Diaz-Mendoza, Mercedes Velasco-Arroyo, Blanca Santamaria, M. Estrella Diaz, Isabel Martinez, Manuel Front Plant Sci Plant Science Co-evolutionary processes in plant–pathogen/herbivore systems indicate that protease inhibitors have a particular value in biotic interactions. However, little is known about the defensive role of their targets, the plant proteases. C1A cysteine proteases are the most abundant enzymes responsible for the proteolytic activity during different processes like germination, development and senescence in plants. To identify and characterize C1A cysteine proteases of barley with a potential role in defense, mRNA and protein expression patterns were analyzed in response to biotics stresses. A barley cysteine protease, HvPap-1, previously related to abiotic stresses and grain germination, was particularly induced by flagellin or chitosan elicitation, and biotic stresses such as the phytopathogenic fungus Magnaporthe oryzae or the phytophagous mite Tetranychus urticae. To elucidate the in vivo participation of this enzyme in defense, transformed barley plants overexpressing or silencing HvPap-1 encoding gene were subjected to M. oryzae infection or T. urticae infestation. Whereas overexpressing plants were less susceptible to the fungus than silencing plants, the opposite behavior occurred to the mite. This unexpected result highlights the complexity of the regulatory events leading to the response to a particular biotic stress. Frontiers Media S.A. 2017-09-12 /pmc/articles/PMC5601043/ /pubmed/28955371 http://dx.doi.org/10.3389/fpls.2017.01585 Text en Copyright © 2017 Diaz-Mendoza, Velasco-Arroyo, Santamaria, Diaz and Martinez. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Diaz-Mendoza, Mercedes
Velasco-Arroyo, Blanca
Santamaria, M. Estrella
Diaz, Isabel
Martinez, Manuel
HvPap-1 C1A Protease Participates Differentially in the Barley Response to a Pathogen and an Herbivore
title HvPap-1 C1A Protease Participates Differentially in the Barley Response to a Pathogen and an Herbivore
title_full HvPap-1 C1A Protease Participates Differentially in the Barley Response to a Pathogen and an Herbivore
title_fullStr HvPap-1 C1A Protease Participates Differentially in the Barley Response to a Pathogen and an Herbivore
title_full_unstemmed HvPap-1 C1A Protease Participates Differentially in the Barley Response to a Pathogen and an Herbivore
title_short HvPap-1 C1A Protease Participates Differentially in the Barley Response to a Pathogen and an Herbivore
title_sort hvpap-1 c1a protease participates differentially in the barley response to a pathogen and an herbivore
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5601043/
https://www.ncbi.nlm.nih.gov/pubmed/28955371
http://dx.doi.org/10.3389/fpls.2017.01585
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