OsHYPK/NatA-mediated N-terminal acetylation regulates the homeostasis of NLR immune protein to fine-tune rice immune responses and growth
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...
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| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2025-05-01
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| Series: | Cell Reports |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124725004905 |
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| Summary: | 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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| ISSN: | 2211-1247 |