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Martinez-D’Alto, Alejandra, Yan, Xia, Detomasi, Tyler C., Sayler, Richard I., Thomas, William C., Talbot, Nicholas J. 
ORCID: https://orcid.org/0000-0001-6434-7757 and Marletta, Michael A.
(2023)
Characterization of a unique polysaccharide monooxygenase from the plant pathogen Magnaporthe oryzae.
Proceedings of the National Academy of Sciences of the United States of America, 120 (8).
ISSN 0027-8424
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Abstract
Blast disease in cereal plants is caused by the fungus Magnaporthe oryzae and accounts for a significant loss in food crops. At the outset of infection, expression of a putative polysaccharide monooxygenase (MoPMO9A) is increased. MoPMO9A contains a catalytic domain predicted to act on cellulose and a carbohydrate-binding domain that binds chitin. A sequence similarity network of the MoPMO9A family AA9 showed that 220 of the 223 sequences in the MoPMO9A-containing cluster of sequences have a conserved unannotated region with no assigned function. Expression and purification of the full length and two MoPMO9A truncations, one containing the catalytic domain and the domain of unknown function (DUF) and one with only the catalytic domain, were carried out. In contrast to other AA9 polysaccharide monooxygenases (PMOs), MoPMO9A is not active on cellulose but showed activity on cereal-derived mixed (1→3, 1→4)-β-D-glucans (MBG). Moreover, the DUF is required for activity. MoPMO9A exhibits activity consistent with C4 oxidation of the polysaccharide and can utilize either oxygen or hydrogen peroxide as a cosubstrate. It contains a predicted 3-dimensional fold characteristic of other PMOs. The DUF is predicted to form a coiled-coil with six absolutely conserved cysteines acting as a zipper between the two α-helices. MoPMO9A substrate specificity and domain architecture are different from previously characterized AA9 PMOs. The results, including a gene ontology analysis, support a role for MoPMO9A in MBG degradation during plant infection. Consistent with this analysis, deletion of MoPMO9A results in reduced pathogenicity.
| Item Type: | Article |
|---|---|
| Additional Information: | Data, Materials, and Software Availability: All study data are included in the article and/or SI Appendix. Funding Information: Support from the NIH project ALS-ENABLE (P30 GM124169) and a High-End Instrumentation Grant S10OD018483. A.M.-D. and T.C.D. were supported by the NSF grant CHE-1904540. T.C.D. was also supported by the NSF grant MCB-1818283. R.I.S acknowledges NIH grant F32-GM143897. We thank the Li Chair Fund to W.C.T and The Gatsby Charitable Foundation to N.J.T. |
| Uncontrolled Keywords: | blast disease,magnaporthe oryzae,polysaccharide monooxygenase,general ,/dk/atira/pure/subjectarea/asjc/1000 |
| Faculty \ School: | Faculty of Science > The Sainsbury Laboratory |
| UEA Research Groups: | Faculty of Medicine and Health Sciences > Research Centres > Norwich Institute for Healthy Aging |
| Related URLs: | |
| Depositing User: | LivePure Connector |
| Date Deposited: | 31 Oct 2024 11:30 |
| Last Modified: | 03 Nov 2024 07:30 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/97361 |
| DOI: | 10.1073/pnas.2215426120 |
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