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Modular structure of HEL protein from Arabidopsis reveals new potential functions for PR-4 proteins.

Biological chemistry (2013-03-06)
Laura Bertini, Silvia Proietti, Maria Pia Aleandri, Francesca Mondello, Silvia Sandini, Carlo Caporale, Carla Caruso
ABSTRACT

Plants possess an innate immune system enabling them to defend themselves against pathogen attack.The accumulation of newly synthesized pathogenesis related proteins (PRs) is one of the most studied inducible plant defence response. In this paper, we report on the characterization of a class I PR4 vacuolar protein from Arabidopsis, named At HEL. The protein has a modular structure consisting of an N-terminal hevein-like domain(CB-HEL) and a C-terminal domain (CD-HEL) that are posttranslationally processed. Both domains show a strong antifungal activity, but they do not have chitinolitic properties.CD-HEL was found to be endowed with RNase, but not DNase activity. Molecular modeling carried out on both domains revealed that CB-HEL possesses a chitin binding site strictly conserved between hevein-type peptides and that the cavity involved in substrate interaction of CD-HEL do not show any residue substitution with respect to the orthologous wheatwin1 from wheat. Using a fishing for partners approach, CB-HEL was found to interact with a fungal fruiting body lectin. According to literature, we can hypothesize that CB-HEL could cross the pathogen hyphal membrane and that its interaction with a fungal lectin could knock out one of the weapons that the fungus uses.

MATERIALS
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Product Description

Sigma-Aldrich
灰链霉菌来源几丁质酶, lyophilized powder (essentially salt free), ≥200 units/g solid
Sigma-Aldrich
壳质酶 来源于绿色木霉, lyophilized powder, ≥600 units/g solid