Comparative analysis on natural variants of fire blight resistance protein FB_MR5 indicates distinct effector recognition mechanisms.

Autor:	Kim H; Plant Immunity Research Center, Seoul National University, Seoul 08826, Republic of Korea. Electronic address: haseongkim@snu.ac.kr., Kim J; Plant Immunity Research Center, Seoul National University, Seoul 08826, Republic of Korea; Department of Agricultural Biotechnology, Seoul National University, Seoul 08826, Republic of Korea. Electronic address: jieun.kim21@snu.ac.kr., Kim M; Department of Life Sciences, Pohang University of Science and Technology, Pohang 37673, Republic of Korea. Electronic address: tjsl1011@gmail.com., Park JT; Apple Research Institute, National Institute of Horticultural & Herbal Science, Gunwi 39000, Republic of Korea. Electronic address: jongtaek@korea.kr., Sohn KH; Plant Immunity Research Center, Seoul National University, Seoul 08826, Republic of Korea; Department of Agricultural Biotechnology, Seoul National University, Seoul 08826, Republic of Korea; Research Institute of Agriculture and Life Sciences, Seoul National University, Seoul 08826, Republic of Korea; Plant Genomics and Breeding Institute, Seoul National University, Seoul 08826, Republic of Korea. Electronic address: keehoon.sohn@snu.ac.kr.
Jazyk:	angličtina
Zdroj:	Molecules and cells [Mol Cells] 2024 Aug; Vol. 47 (8), pp. 100094. Date of Electronic Publication: 2024 Jul 17.
DOI:	10.1016/j.mocell.2024.100094
Abstrakt:	FB_MR5 is a nucleotide-binding domain and leucine-rich repeat protein identified from wild apple species Malus × robusta 5 conferring disease resistance to bacterial fire blight. FB_MR5 (hereafter MrMR5) recognizes the cysteine protease effector EaAvrRpt2 secreted from the causal agent of bacterial fire blight, Erwinia amylovora. We previously reported that MrMR5 is activated by the C-terminal cleavage product (ACP3) of Malus domestica RIN4 (MdRIN4) produced by EaAvrRpt2-directed proteolysis. We show that MbMR5 from a wild apple species Malus baccata shares 99.4% amino acid sequence identity with MrMR5. Surprisingly, transient expression of MbMR5 in Nicotiana benthamiana showed autoactivity in contrast to MrMR5. Domain swap and mutational analyses revealed that 1 amino acid polymorphism in the MbMR5 CC domain is critical in enhancing autoactivity. We further demonstrated that MrMR5 carrying 7 amino acid polymorphisms present in MbMR5 is not activated by MdRIN4 ACP3 but recognizes AvrRpt2 without MdRIN4 in N. benthamiana. Our findings indicate that naturally occurring polymorphisms of MR5 natural variants can confer its cell death-inducing activity and the effector recognition mechanism likely due to altered compatibility with RIN4. Competing Interests: Declaration of Competing Interests The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. The author is an Editorial Board Member/Editor-in-Chief/Associate Editor/Guest Editor for Molecules and Cells and was not involved in the editorial review or the decision to publish this article. (Copyright © 2024 The Author(s). Published by Elsevier Inc. All rights reserved.)
Databáze:	MEDLINE
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