4.7 Article

DEVDase activity is induced in potato leaves during Phytophthora infestans infection

Journal

PLANT PHYSIOLOGY AND BIOCHEMISTRY
Volume 61, Issue -, Pages 197-203

Publisher

ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.plaphy.2012.10.007

Keywords

DEVDase; Plant caspases; Potato; P. infestans; Apoplastic proteins

Categories

Funding

  1. National Scientific and Technical Research Council grant (CONICET)
  2. Scientific Research Commission of the Province of Buenos Aires (CIC)
  3. University of Mar del Plata grant

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Programmed cell death (PCD) occurs in plants, animals and several branches of unicellular eukaryotes as a part of developmental and/or defense processes. Caspase proteases are universal mediators of animal apoptosis, a type of PCD. In plants, there are not animal caspase homologs; therefore, the characterization of caspase-like activities is of considerable importance to our understanding of PCD in plants. Here we report for the first time the involvement of caspase-3-like activity in the resistance mechanism of potato to Phytophthora infestans infection. We showed that disease development in infected potato leaves is dependent of caspase-3-like activity. Unlike plant DEVDases previously reported, this DEVDase activity was sensitive to the serine protease inhibitor PMSF. As reported for other subtilisin- like proteases with caspase activity, potato DEVDase activity was mainly localized in the apoplast. We demonstrated that in total protein extract DEVDase activity accounts for a 60% of serine proteases: however, this percentage increases to 100% in the apoplast. Additionally, this caspase-3-like activity is constitutively expressed in the apoplast of potato leaves. Total DEVDase activity is induced only in potato cultivars with high field resistance to P. infestans. These results show that potato caspase-3-like protease could constitute a tool in the potato defense mechanisms resulting in partial resistance, although further assays would be necessary in order to elucidate its role. (C) 2012 Elsevier Masson SAS. All rights reserved.

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