Academic Journal
Insights into peculiar fungal LPMO family members holding a short C-terminal sequence reminiscent of phosphate binding motifs
| العنوان: | Insights into peculiar fungal LPMO family members holding a short C-terminal sequence reminiscent of phosphate binding motifs |
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| المؤلفون: | Jean-Lou Reyre, Sacha Grisel, Mireille Haon, Ruite Xiang, Jean-Charles Gaillard, Jean Armengaud, Victor Guallar, Antoine Margeot, Simon Arragain, Jean-Guy Berrin, Bastien Bissaro |
| المصدر: | Scientific Reports, Vol 13, Iss 1, Pp 1-14 (2023) |
| بيانات النشر: | Nature Portfolio, 2023. |
| سنة النشر: | 2023 |
| المجموعة: | LCC:Medicine LCC:Science |
| مصطلحات موضوعية: | Medicine, Science |
| الوصف: | Abstract Lytic polysaccharide monooxygenases (LPMOs) are taxonomically widespread copper-enzymes boosting biopolymers conversion (e.g. cellulose, chitin) in Nature. White-rot Polyporales, which are major fungal wood decayers, may possess up to 60 LPMO-encoding genes belonging to the auxiliary activities family 9 (AA9). Yet, the functional relevance of such multiplicity remains to be uncovered. Previous comparative transcriptomic studies of six Polyporales fungi grown on cellulosic substrates had shown the overexpression of numerous AA9-encoding genes, including some holding a C-terminal domain of unknown function (“X282”). Here, after carrying out structural predictions and phylogenetic analyses, we selected and characterized six AA9-X282s with different C-term modularities and atypical features hitherto unreported. Unexpectedly, after screening a large array of conditions, these AA9-X282s showed only weak binding properties to cellulose, and low to no cellulolytic oxidative activity. Strikingly, proteomic analysis revealed the presence of multiple phosphorylated residues at the surface of these AA9-X282s, including a conserved residue next to the copper site. Further analyses focusing on a 9 residues glycine-rich C-term extension suggested that it could hold phosphate-binding properties. Our results question the involvement of these AA9 proteins in the degradation of plant cell wall and open new avenues as to the divergence of function of some AA9 members. |
| نوع الوثيقة: | article |
| وصف الملف: | electronic resource |
| اللغة: | English |
| تدمد: | 2045-2322 |
| Relation: | https://doaj.org/toc/2045-2322 |
| DOI: | 10.1038/s41598-023-38617-5 |
| URL الوصول: | https://doaj.org/article/a3b79ba391f840a3b1a62f2b18c38065 |
| رقم الانضمام: | edsdoj.3b79ba391f840a3b1a62f2b18c38065 |
| قاعدة البيانات: | Directory of Open Access Journals |
Full Text Finder | تدمد: | 20452322 |
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| DOI: | 10.1038/s41598-023-38617-5 |