Distinct domains of the AVRPM3A2/F2 avirulence protein from wheat powdery mildew are involved in immune receptor recognition and putative effector function

Distinct domains of the AVRPM3A2/F2 avirulence protein from wheat powdery mildew are involved in immune receptor recognition and putative effector function

© 2018 The Authors. New Phytologist © 2018 New Phytologist Trust.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 218(2018), 2 vom: 24. Apr., Seite 681-695
1. Verfasser: McNally, Kaitlin Elyse (VerfasserIn)
Weitere Verfasser: Menardo, Fabrizio, Lüthi, Linda, Praz, Coraline Rosalie, Müller, Marion Claudia, Kunz, Lukas, Ben-David, Roi, Chandrasekhar, Kottakota, Dinoor, Amos, Cowger, Christina, Meyers, Emily, Xue, Mingfeng, Zeng, Fangsong, Gong, Shuangjun, Yu, Dazhao, Bourras, Salim, Keller, Beat
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2018
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Blumeria graminis Nicotiana benthamiana Pm3 avirulence gene gene synthesis natural diversity site-directed mutagenesis wheat mehr... Fungal Proteins Plant Proteins Receptors, Immunologic
Beschreibung
Zusammenfassung:© 2018 The Authors. New Phytologist © 2018 New Phytologist Trust.
Recognition of the AVRPM3A2/F2 avirulence protein from powdery mildew by the wheat PM3A/F immune receptor induces a hypersensitive response after co-expression in Nicotiana benthamiana. The molecular determinants of this interaction and how they shape natural AvrPm3a2/f2 allelic diversity are unknown. We sequenced the AvrPm3a2/f2 gene in a worldwide collection of 272 mildew isolates. Using the natural polymorphisms of AvrPm3a2/f2 as well as sequence information from related gene family members, we tested 85 single-residue-altered AVRPM3A2/F2 variants with PM3A, PM3F and PM3FL456P/Y458H (modified for improved signaling) in Nicotiana benthamiana for effects on recognition. An intact AvrPm3a2/f2 gene was found in all analyzed isolates and the protein variant recognized by PM3A/F occurred globally at high frequencies. Single-residue alterations in AVRPM3A2/F2 mostly disrupted, but occasionally enhanced, the recognition response by PM3A, PM3F and PM3FL456P/Y458H . Residues enhancing hypersensitive responses constituted a protein domain separate from both naturally occurring polymorphisms and positively selected residues of the gene family. These results demonstrate the utility of using gene family sequence diversity to screen residues for their role in recognition. This approach identified a putative interaction surface in AVRPM3A2/F2 not polymorphic in natural alleles. We conclude that molecular mechanisms besides recognition drive AvrPm3a2/f2 diversification
Beschreibung:Date Completed 19.09.2019
Date Revised 13.11.2024
published: Print-Electronic
GENBANK: MG739404, MG739429
Citation Status MEDLINE
ISSN:1469-8137
DOI:10.1111/nph.15026