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Crystal structure of the Melampsora lini effector AvrP reveals insights into a possible nuclear function and recognition by the flax disease resistance protein P

Zhang, XiaoXiao; Farah, Nadya; Rolston, Laura; Ericsson, Daniel J.; Catanzariti, Ann-Maree; Bernoux, Maud; Ve, Thomas; Bendak, Katerina; Chen, Chunhong; Mackay, Joel P.; Lawrence, Gregory J.; Hardham, Adrienne; Ellis, Jeffrey G.; Williams, Simon; Dodds, Peter N.; Jones, David; Kobe, Bostjan

Description

The effector protein AvrP is secreted by the flax rust fungal pathogen (Melampsora lini) and recognized specifically by the flax (Linum usitatissimum) P disease resistance protein, leading to effector‐triggered immunity. To investigate the biological function of this effector and the mechanisms of specific recognition by the P resistance protein, we determined the crystal structure of AvrP. The structure reveals an elongated zinc‐finger‐like structure with a novel interleaved zinc‐binding...[Show more]

dc.contributor.authorZhang, XiaoXiao
dc.contributor.authorFarah, Nadya
dc.contributor.authorRolston, Laura
dc.contributor.authorEricsson, Daniel J.
dc.contributor.authorCatanzariti, Ann-Maree
dc.contributor.authorBernoux, Maud
dc.contributor.authorVe, Thomas
dc.contributor.authorBendak, Katerina
dc.contributor.authorChen, Chunhong
dc.contributor.authorMackay, Joel P.
dc.contributor.authorLawrence, Gregory J.
dc.contributor.authorHardham, Adrienne
dc.contributor.authorEllis, Jeffrey G.
dc.contributor.authorWilliams, Simon
dc.contributor.authorDodds, Peter N.
dc.contributor.authorJones, David
dc.contributor.authorKobe, Bostjan
dc.date.accessioned2021-05-12T01:57:00Z
dc.date.available2021-05-12T01:57:00Z
dc.identifier.issn1464-6722
dc.identifier.urihttp://hdl.handle.net/1885/232677
dc.description.abstractThe effector protein AvrP is secreted by the flax rust fungal pathogen (Melampsora lini) and recognized specifically by the flax (Linum usitatissimum) P disease resistance protein, leading to effector‐triggered immunity. To investigate the biological function of this effector and the mechanisms of specific recognition by the P resistance protein, we determined the crystal structure of AvrP. The structure reveals an elongated zinc‐finger‐like structure with a novel interleaved zinc‐binding topology. The residues responsible for zinc binding are conserved in AvrP effector variants and mutations of these motifs result in a loss of P‐mediated recognition. The first zinc‐coordinating region of the structure displays a positively charged surface and shows some limited similarities to nucleic acid‐binding and chromatin‐associated proteins. We show that the majority of the AvrP protein accumulates in the plant nucleus when transiently expressed in Nicotiana benthamiana cells, suggesting a nuclear pathogenic function. Polymorphic residues in AvrP and its allelic variants map to the protein surface and could be associated with differences in recognition specificity. Several point mutations of residues on the non‐conserved surface patch result in a loss of recognition by P, suggesting that these residues are required for recognition.
dc.description.sponsorshipThis research was supported by Australian Research Council (ARC) Discovery Projects DP120100685, DP130104098 and DP160102244. XZ was a recipient of an ANZ Trustees PhD Scholarship for Medical Research in Queensland. BK is a National Health and Medical Research Council (NHMRC) Principal Research Fellow (1003325 and 1110971). MB was a recipient of an ARC Discovery Early Career Research Award (DE130101292).
dc.format.mimetypeapplication/pdf
dc.language.isoen_AU
dc.publisherBlackwell Publishing Ltd
dc.rights© 2017 BSPP and John Wiley & Songs Ltd
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.sourceMolecular Plant Pathology
dc.subjectcrystal structure
dc.subjecteffector-triggered immunity
dc.subjectflax rust (Melampsora lini) effector
dc.subjectNLR [nucleotide-binding and oligomerization domain (NOD)-like receptor, nucleotide-binding/ leucine-rich repeat receptor]
dc.subjectnuclear localization
dc.subjectplant disease resistance
dc.subjectzinc finger
dc.titleCrystal structure of the Melampsora lini effector AvrP reveals insights into a possible nuclear function and recognition by the flax disease resistance protein P
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume19
dc.date.issued2017-11-16
local.identifier.absfor060109 - Proteomics and Intermolecular Interactions (excl. Medical Proteomics)
local.identifier.absfor060112 - Structural Biology (incl. Macromolecular Modelling)
local.identifier.absfor060702 - Plant Cell and Molecular Biology
local.identifier.ariespublicationa383154xPUB9192
local.publisher.urlhttps://bsppjournals.onlinelibrary.wiley.com/
local.type.statusPublished Version
local.contributor.affiliationZhang, XiaoXiao, University of Queensland
local.contributor.affiliationFarah, Nadya, College of Science, ANU
local.contributor.affiliationRolston, Laura, College of Science, ANU
local.contributor.affiliationEricsson, Daniel J., University of Queensland
local.contributor.affiliationCatanzariti, Ann-Maree, College of Science, ANU
local.contributor.affiliationBernoux, Maud, CSIRO
local.contributor.affiliationVe, Thomas, University of Queensland
local.contributor.affiliationBendak, Katerina, University of Sydney
local.contributor.affiliationChen, Chunhong, CSIRO Agriculture
local.contributor.affiliationMackay, Joel P., University of Sydney
local.contributor.affiliationLawrence, Gregory J., CSIRO Plant Industry
local.contributor.affiliationHardham, Adrienne, College of Science, ANU
local.contributor.affiliationEllis, Jeffrey G., CSIRO Division of Plant Industry
local.contributor.affiliationWilliams, Simon, College of Science, ANU
local.contributor.affiliationDodds, Peter N., CSIRO
local.contributor.affiliationJones, David, College of Science, ANU
local.contributor.affiliationKobe, Bostjan, University of Queensland
dc.relationhttp://purl.org/au-research/grants/arc/DP120100685
dc.relationhttp://purl.org/au-research/grants/arc/DP130104098
dc.relationhttp://purl.org/au-research/grants/arc/DP160102244
dc.relationhttp://purl.org/au-research/grants/nhmrc/1003325
dc.relationhttp://purl.org/au-research/grants/nhmrc/1110971
dc.relationhttp://purl.org/au-research/grants/arc/DE130101292
local.bibliographicCitation.issue5
local.bibliographicCitation.startpage1196
local.bibliographicCitation.lastpage1209
local.identifier.doi10.1111/mpp.12597
local.identifier.absseo820299 - Horticultural Crops not elsewhere classified
dc.date.updated2020-11-23T11:38:00Z
local.identifier.scopusID2-s2.0-85034222061
dcterms.accessRightsOpen Access
dc.provenancehttps://v2.sherpa.ac.uk/id/publication/7107..."Published version can be made open access on institutional repository with CC BY-NC-ND license" from SHERPA/RoMEO site (as at 12.5.2021).
dc.rights.licenseCreative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)
CollectionsANU Research Publications

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