A kinase fusion protein from Aegilops longissima confers resistance to wheat powdery mildew

Huagang He (), Zhaozhao Chen, Renchun Fan, Jie Zhang, Shanying Zhu, Jiale Wang, Qianyuan Zhang, Anli Gao, Shuangjun Gong, Lu Zhang, Yanan Li, Yitong Zhao, Simon G. Krattinger, Qian-Hua Shen, Hongjie Li and Yajun Wang ()
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Huagang He: Jiangsu University
Zhaozhao Chen: Jiangsu University
Renchun Fan: Chinese Academy of Sciences
Jie Zhang: Sichuan Academy of Agricultural Sciences
Shanying Zhu: Jiangsu University
Jiale Wang: Jiangsu University
Qianyuan Zhang: Jiangsu University
Anli Gao: Henan University
Shuangjun Gong: Hubei Academy of Agricultural Sciences
Lu Zhang: Chinese Academy of Sciences
Yanan Li: Chinese Academy of Sciences
Yitong Zhao: Chinese Academy of Sciences
Simon G. Krattinger: King Abdullah University of Science and Technology (KAUST)
Qian-Hua Shen: Chinese Academy of Sciences
Hongjie Li: Xianghu Laboratory
Yajun Wang: Chinese Academy of Sciences

Nature Communications, 2024, vol. 15, issue 1, 1-13

Abstract: Abstract Many disease resistance genes have been introgressed into wheat from its wild relatives. However, reduced recombination within the introgressed segments hinders the cloning of the introgressed genes. Here, we have cloned the powdery mildew resistance gene Pm13, which is introgressed into wheat from Aegilops longissima, using a method that combines physical mapping with radiation-induced chromosomal aberrations and transcriptome sequencing analysis of ethyl methanesulfonate (EMS)-induced loss-of-function mutants. Pm13 encodes a kinase fusion protein, designated MLKL-K, with an N-terminal domain of mixed lineage kinase domain-like protein (MLKL_NTD domain) and a C-terminal serine/threonine kinase domain bridged by a brace. The resistance function of Pm13 is validated through transient and stable transgenic complementation assays. Transient over-expression analyses in Nicotiana benthamiana leaves and wheat protoplasts reveal that the fragment Brace-Kinase122-476 of MLKL-K is capable of inducing cell death, which is dependent on a functional kinase domain and the three α-helices in the brace region close to the N-terminus of the kinase domain.

Date: 2024
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DOI: 10.1038/s41467-024-50909-6

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