The C-terminal intrinsically disordered region of a fungal lytic polysaccharide monooxygenase binds copper and displays anti-fungal properties
Abstract
Lytic Polysaccharide Monooxygenases (LPMOs) are enzymes that play a crucial role in the degradation of complex polysaccharides such as cellulose and chitin. While LPMOs have attracted significant interest for industrial applications to convert biomass into biofuels, emerging evidence suggests alternative functions in fungal plant pathogenesis, microbial diseases and (micro)organism development. The AA14 LPMO family is widely distributed in filamentous fungi but remains enigmatic as its initially-suspected substrate specificity was recently challenged. Moreover, more than half of AA14 family members display a disordered C-terminal region (dCTR), hypothesized to have functional relevance. In this study, we functionally characterized the Pycnoporus coccineus AA14A LPMO that harbors a dCTR. We used small angle X-ray scattering (SAXS) and circular dichroism to show that its dCTR is highly disordered. It consists of a heavily glycosylated low complexity region followed by a charged C-terminal tail. We uncovered that the PcoAA14A dCTR binds copper ions through histidine residues located in the C-terminal tail. Using electron paramagnetic resonance (EPR), we further showed that an oxidative process involving copper and a redox-sensitive cysteine triggers enzyme dimerization. Noting similarities between the last residues of the C-terminal tail and antimicrobial peptides, we investigated its potential antimicrobial function. We found that the positively charged region of the C-terminal tail selectively inhibits the growth of basidiomycete fungal spores. These data reveal that the dCTRs appended to AA14 LPMOs are functional regions that must be considered to unveil the role of these atypical LPMOs.
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BibTeX
@article{tamburrini2026cterminal,
title = {{The C-terminal intrinsically disordered region of a fungal lytic polysaccharide monooxygenase binds copper and displays anti-fungal properties}},
author = {Ketty C Tamburrini and Koar Chorozian and Clarisse Roblin and Aurore Labourel and Mireille Haon and Sacha Grisel and Evangelos Topakas and Mickael Lafond and Bruno Guigliarelli and Gaston Courtade and Sonia Longhi and Jean-Guy Berrin},
journal = {International Journal of Biological Macromolecules},
year = {2026},
month = oct,
doi = {10.1016/j.ijbiomac.2026.152439},
url = {https://hal.science/hal-05845654v1},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - The C-terminal intrinsically disordered region of a fungal lytic polysaccharide monooxygenase binds copper and displays anti-fungal properties
AU - Ketty C Tamburrini
AU - Koar Chorozian
AU - Clarisse Roblin
AU - Aurore Labourel
AU - Mireille Haon
AU - Sacha Grisel
AU - Evangelos Topakas
AU - Mickael Lafond
AU - Bruno Guigliarelli
AU - Gaston Courtade
AU - Sonia Longhi
AU - Jean-Guy Berrin
PY - 2026
DA - 2026/10/30
JO - International Journal of Biological Macromolecules
DO - 10.1016/j.ijbiomac.2026.152439
UR - https://hal.science/hal-05845654v1
AB - Lytic Polysaccharide Monooxygenases (LPMOs) are enzymes that play a crucial role in the degradation of complex polysaccharides such as cellulose and chitin. While LPMOs have attracted significant interest for industrial applications to convert biomass into biofuels, emerging evidence suggests alternative functions in fungal plant pathogenesis, microbial diseases and (micro)organism development. The AA14 LPMO family is widely distributed in filamentous fungi but remains enigmatic as its initially-suspected substrate specificity was recently challenged. Moreover, more than half of AA14 family members display a disordered C-terminal region (dCTR), hypothesized to have functional relevance. In this study, we functionally characterized the Pycnoporus coccineus AA14A LPMO that harbors a dCTR. We used small angle X-ray scattering (SAXS) and circular dichroism to show that its dCTR is highly disordered. It consists of a heavily glycosylated low complexity region followed by a charged C-terminal tail. We uncovered that the PcoAA14A dCTR binds copper ions through histidine residues located in the C-terminal tail. Using electron paramagnetic resonance (EPR), we further showed that an oxidative process involving copper and a redox-sensitive cysteine triggers enzyme dimerization. Noting similarities between the last residues of the C-terminal tail and antimicrobial peptides, we investigated its potential antimicrobial function. We found that the positively charged region of the C-terminal tail selectively inhibits the growth of basidiomycete fungal spores. These data reveal that the dCTRs appended to AA14 LPMOs are functional regions that must be considered to unveil the role of these atypical LPMOs.
SN - 0141-8130
ER -