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OsHYPK/NatA-mediated N-terminal acetylation regulates the homeostasis of NLR immune protein to fine-tune rice immune responses and growth

Keeping nucleotide-binding leucine-rich repeat (NLR) protein at appropriate levels is critical for plant survival. Huntingtin Yeast Partner K (OsHYPK) was previously identified as a positive regulator of N-terminal acetyltransferase A (NatA) activity in rice. Here, we find that oshypk shows enhanced...

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Hauptverfasser: Huang, Yaqian (VerfasserIn) , Gong, Xiaodi (VerfasserIn) , Shi, Hui (VerfasserIn) , Wang, Peiyi (VerfasserIn) , Yuan, Yundong (VerfasserIn) , Kong, Cuilian (VerfasserIn) , Zhou, Jie (VerfasserIn) , Wu, Dianxing (VerfasserIn) , Liang, Yan (VerfasserIn) , Wang, Yonghong (VerfasserIn) , Wang, Jing (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: May 15,2025
In: Cell reports
Year: 2025, Jahrgang: 44, Heft: 5, Pages: 1-18
ISSN:2211-1247
DOI:10.1016/j.celrep.2025.115719
Online-Zugang:Verlag, kostenfrei, Volltext: https://doi.org/10.1016/j.celrep.2025.115719
Verlag, kostenfrei, Volltext: https://www.sciencedirect.com/science/article/pii/S2211124725004905
Volltext
Verfasserangaben:Yaqian Huang, Xiaodi Gong, Hui Shi, Peiyi Wang, Yundong Yuan, Cuilian Kong, Jie Zhou, Dianxing Wu, Yan Liang, Yonghong Wang, Jing Wang

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520 |a Keeping nucleotide-binding leucine-rich repeat (NLR) protein at appropriate levels is critical for plant survival. Huntingtin Yeast Partner K (OsHYPK) was previously identified as a positive regulator of N-terminal acetyltransferase A (NatA) activity in rice. Here, we find that oshypk shows enhanced resistance to Magnaporthe oryzae (M. oryzae). Through screening for suppressors of oshypk (soh), we identify suppressor soh74, which contains a mutation in RESISTANCE TO P. SYRINGAE PV MACULICOLA1 (RPM1)-like NLR protein (RPM1-L1) and exhibits compromised resistance to M. oryzae. Mechanistically, declined N-terminal acetylation (NTA) degree in oshypk leads to protein accumulation of RPM1-L1, contributing to enhanced disease resistance. To restrict RPM1-L1 accumulation, OsHYPK is expressed at high levels under normal conditions. However, pathogen infection reduces OsHYPK level to release the inhibition on RPM1-L1, leading to immune activation. This study reveals a vital pathway in which OsHYPK/NatA-mediated NTA rapidly fine-tunes NLR-mediated immune response. 
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