An HMA-like integrated domain in the wheat tandem kinase WTK4 recognises an RNase-like pathogen effector
12 affiliations
- 1Department of Plant and Microbial Biology, University of Zürich, Zürich, Switzerland
- 2University of Zurich
- 3Plant Science Program, Biological and Environmental Science and Engineering Division (BESE), King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia
- 4King Abdullah University of Science and Technology (KAUST)
- 5Department of Microbiology and Genetics, Spanish-Portuguese Agricultural Research Centre (CIALE), University of Salamanca, Salamanca, Spain
- 6University of Salamanca
- 7Chair of Phytopathology, TUM School of Life Sciences, Technical University of Munich, Freising, Germany
- 8TUM School of Life Sciences
- 9Department of Plant and Microbial Biology, University of Zürich, Zürich, Switzerland. [email protected]
- 10Department of Microbiology and Genetics, Spanish-Portuguese Agricultural Research Centre (CIALE), University of Salamanca, Salamanca, Spain. [email protected]
- 11Department of Plant and Microbial Biology, University of Zürich, Zürich, Switzerland. [email protected]
- 12Research Unit of Excellence "Agricultural Production and Environment" (AGRIENVIRONMENT), University of Salamanca, Salamanca, Spain. [email protected]
Abstract
Proteins with a tandem kinase structure have recently emerged as players in race-specific resistance in cereal crops. However, the molecular understanding of these immune receptors' resistance mechanisms is limited by the lack of knowledge about the pathogen effectors that they recognise. In this work, we identify AvrWTK4, the wheat powdery mildew RNase-like effector recognised by the wheat tandem kinase protein WTK4, through a combination of bi-parental genetic mapping and mutagenesis. We demonstrate that mutations in the AvrWTK4 gene or a reduction of its expression lead to virulence on WTK4. Transfection of AvrWTK4 specifically induced cell death in WTK4-expressing Aegilops tauschii protoplasts. The avirulent AvrWTK4 variant interacts more strongly than the virulent variant with the N-terminal heavy metal-associated (HMA)-like domain of WTK4. We found that the integrated HMA-like domain possibly serves as a direct effector-binding decoy for WTK4, providing a mechanistic paradigm for effector recognition by tandem kinase proteins.
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BibTeX
@article{bernasconi2026hmalike,
title = {{An HMA-like integrated domain in the wheat tandem kinase WTK4 recognises an RNase-like pathogen effector}},
author = {Zoe Bernasconi and Ursin Stirnemann and Yang Xu and Aline Herger and Renjie Chen and Victoria Widrig and Matthias Heuberger and Mariantonietta Lettieri and Marion Claudia Müller and Brande B. H. Wulff and Thomas Wicker and Beat Keller and Javier Sánchez‐Martín},
journal = {Nature Communications},
year = {2026},
month = jul,
doi = {10.1038/s41467-026-74940-x},
url = {https://doi.org/10.1038/s41467-026-74940-x},
note = {CC BY},
}
RIS
TY - JOUR
TI - An HMA-like integrated domain in the wheat tandem kinase WTK4 recognises an RNase-like pathogen effector
AU - Zoe Bernasconi
AU - Ursin Stirnemann
AU - Yang Xu
AU - Aline Herger
AU - Renjie Chen
AU - Victoria Widrig
AU - Matthias Heuberger
AU - Mariantonietta Lettieri
AU - Marion Claudia Müller
AU - Brande B. H. Wulff
AU - Thomas Wicker
AU - Beat Keller
AU - Javier Sánchez‐Martín
PY - 2026
DA - 2026/07/06
JO - Nature Communications
DO - 10.1038/s41467-026-74940-x
UR - https://doi.org/10.1038/s41467-026-74940-x
AB - Proteins with a tandem kinase structure have recently emerged as players in race-specific resistance in cereal crops. However, the molecular understanding of these immune receptors' resistance mechanisms is limited by the lack of knowledge about the pathogen effectors that they recognise. In this work, we identify AvrWTK4, the wheat powdery mildew RNase-like effector recognised by the wheat tandem kinase protein WTK4, through a combination of bi-parental genetic mapping and mutagenesis. We demonstrate that mutations in the AvrWTK4 gene or a reduction of its expression lead to virulence on WTK4. Transfection of AvrWTK4 specifically induced cell death in WTK4-expressing Aegilops tauschii protoplasts. The avirulent AvrWTK4 variant interacts more strongly than the virulent variant with the N-terminal heavy metal-associated (HMA)-like domain of WTK4. We found that the integrated HMA-like domain possibly serves as a direct effector-binding decoy for WTK4, providing a mechanistic paradigm for effector recognition by tandem kinase proteins.
SN - 2041-1723
ER -