Carbohydrate-binding property of a cell wall integrity and stress response component (WSC) domain of an alcohol oxidase from the rice blast pathogen Pyricularia oryzae

Publication date: Available online 25 February 2019Source: Enzyme and Microbial TechnologyAuthor(s): Shinichi Oide, Yuya Tanaka, Akira Watanabe, Masayuki InuiAbstractThe cell wall integrity and stress response component (WSC) domain was first described in the Wsc-family protein of the yeast Saccharomyces cerevisiae, and later found in diverse eukaryotic organisms. Due solely to their presence in the Wsc-family proteins working as a plasma membrane sensor for surface stress and in a fungal β-1,3-exoglucanse, WSC domains have been presumed to possess carbohydrate-binding property without any experimental evidence. Aiming at elucidation of function(s) of WSC domains, we characterized a WSC domain-containing alcohol oxidase from the rice blast pathogen Pyricularia oryzae (PoAlcOX). Recombinant PoAlcOX produced with Pichia pastoris showed alcohol oxidase activity toward a wide range of substrates including two aliphatic alcohols, a branched-chain alcohol, a diol, and a polyol. Deletion of the WSC domain virtually unaffected oxidation of these substrates by PoAlcOX, indicating that the domain makes no contribution to the catalytic activity. In analogy to some carbohydrate-binding modules, we inferred that the WSC domain plays a role in protein anchoring, and evaluated binding capability of PoAlcOX to a set of polysaccharide components of fungal and plant cell walls. This revealed that PoAlcOX binds to xylans and fungal chitin/β-1,3-glucan in the WSC domain-dependent manner, demon...
Source: Enzyme and Microbial Technology - Category: Biotechnology Source Type: research