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HvPap-1 C1A protease actively participates in barley proteolysis mediated by abiotic stresses
Author(s) -
Blanca VelascoArroyo,
Mercedes DíazMendoza,
Jacinto Gandullo,
Pablo GonzálezMelendi,
M. Estrella Santamaría,
José Domínguez-Figueroa,
Göetz Hensel,
Manuel Martínez,
Jochen Kumlehn,
Isabel Dı́az
Publication year - 2016
Publication title -
journal of experimental botany
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 2.616
H-Index - 242
eISSN - 1460-2431
pISSN - 0022-0957
DOI - 10.1093/jxb/erw212
Subject(s) - proteases , abiotic component , proteolysis , protease , abiotic stress , biology , microbiology and biotechnology , cysteine protease , gene , gene silencing , biochemistry , enzyme , ecology
Protein breakdown and mobilization from old or stressed tissues to growing and sink organs are some of the metabolic features associated with abiotic/biotic stresses, essential for nutrient recycling. The massive degradation of proteins implies numerous proteolytic events in which cysteine-proteases are the most abundant key players. Analysing the role of barley C1A proteases in response to abiotic stresses is crucial due to their impact on plant growth and grain yield and quality. In this study, dark and nitrogen starvation treatments were selected to induce stress in barley. Results show that C1A proteases participate in the proteolytic processes triggered in leaves by both abiotic treatments, which strongly induce the expression of the HvPap-1 gene encoding a cathepsin F-like protease. Differences in biochemical parameters and C1A gene expression were found when comparing transgenic barley plants overexpressing or silencing the HvPap-1 gene and wild-type dark-treated leaves. These findings associated with morphological changes evidence a lifespan-delayed phenotype of HvPap-1 silenced lines. All these data elucidate on the role of this protease family in response to abiotic stresses and the potential of their biotechnological manipulation to control the timing of plant growth.

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