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Characterization of a novel Kazal-type serine proteinase inhibitor of Arabidopsis thaliana.

Authors :
Pariani S
Contreras M
Rossi FR
Sander V
Corigliano MG
Simón F
Busi MV
Gomez-Casati DF
Pieckenstain FL
Duschak VG
Clemente M
Source :
Biochimie [Biochimie] 2016 Apr; Vol. 123, pp. 85-94. Date of Electronic Publication: 2016 Feb 04.
Publication Year :
2016

Abstract

Many different types of serine proteinase inhibitors have been involved in several kinds of plant physiological processes, including defense mechanisms against phytopathogens. Kazal-type serine proteinase inhibitors, which are included in the serine proteinase inhibitor family, are present in several organisms. These proteins play a regulatory role in processes that involve serine proteinases like trypsin, chymotrypsin, thrombin, elastase and/or subtilisin. In the present work, we characterized two putative Kazal-type serine proteinase inhibitors from Arabidopsis thaliana, which have a single putative Kazal-type domain. The expression of these inhibitors is transiently induced in response to leaf infection by Botrytis cinerea, suggesting that they play some role in defense against pathogens. We also evaluated the inhibitory specificity of one of the Kazal-type serine proteinase inhibitors, which resulted to be induced during the local response to B. cinerea infection. The recombinant Kazal-type serine proteinase inhibitor displayed high specificity for elastase and subtilisin, but low specificity for trypsin, suggesting differences in its selectivity. In addition, this inhibitor exhibited a strong antifungal activity inhibiting the germination rate of B. cinerea conidia in vitro. Due to the important role of proteinase inhibitors in plant protection against pathogens and pests, the information about Kazal-type proteinase inhibitors described in the present work could contribute to improving current methods for plant protection against pathogens.<br /> (Copyright © 2016 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.)

Details

Language :
English
ISSN :
1638-6183
Volume :
123
Database :
MEDLINE
Journal :
Biochimie
Publication Type :
Academic Journal
Accession number :
26853817
Full Text :
https://doi.org/10.1016/j.biochi.2016.02.002