Cell Reports (May 2025)

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

  • Yaqian Huang,
  • Xiaodi Gong,
  • Hui Shi,
  • Peiyi Wang,
  • Yundong Yuan,
  • Cuilian Kong,
  • Jie Zhou,
  • Dianxing Wu,
  • Yan Liang,
  • Yonghong Wang,
  • Jing Wang

DOI
https://doi.org/10.1016/j.celrep.2025.115719
Journal volume & issue
Vol. 44, no. 5
p. 115719

Abstract

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Summary: 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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