Structurally distinct Arabidopsis thaliana NLR immune receptors recognize tandem WY domains of an oomycete effector
© 2016 The Authors. New Phytologist © 2016 New Phytologist Trust.
| Veröffentlicht in: | The New phytologist. - 1979. - 210(2016), 3 vom: 04. Mai, Seite 984-96 |
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| Weitere Verfasser: | , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2016
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| Zugriff auf das übergeordnete Werk: | The New phytologist |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. ATR1 Estland (Est-1) Hyaloperonospora arabidopsidis RPP1 Zdarec (Zdr-1) nucleotide binding-leucine rich repeat receptor (NLR) plant immunity mehr... |
| Zusammenfassung: | © 2016 The Authors. New Phytologist © 2016 New Phytologist Trust. Nucleotide-binding leucine-rich repeat (NB-LRR, or NLR) receptors mediate pathogen recognition. The Arabidopsis thaliana NLR RPP1 recognizes the tandem WY-domain effector ATR1 from the oomycete Hyaloperonospora arabidopsidis through direct association with C-terminal LRRs. We isolated and characterized homologous NLR genes RPP1-EstA and RPP1-ZdrA from two Arabidopsis ecotypes, Estland (Est-1) and Zdarec (Zdr-1), responsible for recognizing a novel spectrum of ATR1 alleles. RPP1-EstA and -ZdrA encode nearly identical NLRs that are phylogenetically distinct from known immunity-activating RPP1 homologs and possess greatly expanded LRR domains. Site-directed mutagenesis and truncation analysis of ATR1 suggests that these homologs recognize a novel surface of the 2(nd) WY domain of ATR1, partially specified by a C-terminal region of the LRR domain. Synteny comparison with RPP1 loci involved in hybrid incompatibility suggests that these functions evolved independently. Closely related RPP1 homologs have diversified their recognition spectra through LRR expansion and sequence variation, allowing them to detect multiple surfaces of the same pathogen effector. Engineering NLR receptor specificity may require a similar combination of repeat expansion and tailored amino acid variation |
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| Beschreibung: | Date Completed 26.12.2016 Date Revised 03.12.2021 published: Print-Electronic GENBANK: KT722749, KT722750, KT722751, KT722752 Citation Status MEDLINE |
| ISSN: | 1469-8137 |
| DOI: | 10.1111/nph.13823 |