The disordered C- terminal tail of fungal LPMOs from phytopathogens mediates protein dimerization and impacts plant penetration
成果类型：
Article
署名作者：
Tamburrini, Ketty C.; Kodama, Sayo; Grisel, Sacha; Haon, Mireille; Nishiuchi, Takumi; Bissaro, Bastien; Kubo, Yasuyuki; Longhi, Sonia; Berrin, Jean-Guy
署名单位：
Aix-Marseille Universite; Centre National de la Recherche Scientifique (CNRS); CNRS - National Institute for Biology (INSB); Aix-Marseille Universite; INRAE; Setsunan University; Aix-Marseille Universite; INRAE; Kanazawa University
刊物名称：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
ISSN/ISSBN：
0027-11885
DOI：
10.1073/pnas.2319998121
发表日期：
2024-03-26
关键词：
lytic polysaccharide monooxygenases
denatured proteins
cellulose
copper
degradation
DISCOVERY
cleavage
oxidases
enzymes
nmr
摘要：
Lytic polysaccharide monooxygenases (LPMOs) are monocopper enzymes that oxidatively degrade various polysaccharides, such as cellulose. Despite extensive research on this class of enzymes, the role played by their C- terminal regions predicted to be intrinsically disordered (dCTR) has been overlooked. Here, we investigated the function of the dCTR of an LPMO, called CoAA9A, up- regulated during plant infection by Colletotrichum orbiculare, the causative agent of anthracnose. After recombinant production of the full- length protein, we found that the dCTR mediates CoAA9A dimerization in vitro, via a disulfide bridge, a hitherto- never- reported property that positively affects both binding and activity on cellulose. Using SAXS experiments, we show that the homodimer is in an extended conformation. In vivo, we demonstrate that gene deletion impairs formation of the infection- specialized cell called appressorium and delays penetration of the plant. Using immunochemistry, we show that the protein is a dimer not only in vitro but also in vivo when secreted by the appressorium. As these peculiar LPMOs are also found in other plant pathogens, our findings open up broad avenues for crop protection.