Scholarlink

<p><i>Magnaporthe oryzae</i> snodprot1 homolog (MSP1), a potential PAMP, is known to trigger defense responses in rice. However, the receptor(s) and downstream interacting components of MSP1 in rice have not been identified so far. Using multiple immunoprecipitation–mass spectrometry (IP–MS) analyses in transgenic rice expressing MSP1-YFP, we identified several heat shock proteins (HSPs) as MSP1 interacting partners. Heat stress treatment suppressed MSP1-induced cell death in tobacco plants transiently expressing MSP1. Subsequent IP–MS analysis on these tobacco plants, exposed to heat stress, resulted in the identification of an HSP having a highly conserved sequence to the HSP70 of rice. Co-expression of MSP1 with HSP70 failed to induce cell death in tobacco, confirming the involvement of the HSP70 in the MSP1 immune response. Rice protoplasts, co-expressing MSP1 and HSP70, showed a direct interaction between these two proteins <i>in planta</i>. Taken together, the results reported here highlight the pivotal role of HSP70 in MSP1-induced signaling and enhance our understanding of rice–<i>M. oryzae</i> interaction.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Identification of HSP70 as a Key Regulator of MSP1-Induced Signaling in Rice

  • 期刊论文

  • 发表日期：

    2025年2月15日

查看全文
  • Cheol Woo Min,
  • Jeong Woo Jang,
  • Ju Soon Yoo,
  • Gi Hyun Lee,
  • Yu-Jin Kim,
  • Ravi Gupta,
  • Sun Tae Kim

摘要

Magnaporthe oryzae snodprot1 homolog (MSP1), a potential PAMP, is known to trigger defense responses in rice. However, the receptor(s) and downstream interacting components of MSP1 in rice have not been identified so far. Using multiple immunoprecipitation–mass spectrometry (IP–MS) analyses in transgenic rice expressing MSP1-YFP, we identified several heat shock proteins (HSPs) as MSP1 interacting partners. Heat stress treatment suppressed MSP1-induced cell death in tobacco plants transiently expressing MSP1. Subsequent IP–MS analysis on these tobacco plants, exposed to heat stress, resulted in the identification of an HSP having a highly conserved sequence to the HSP70 of rice. Co-expression of MSP1 with HSP70 failed to induce cell death in tobacco, confirming the involvement of the HSP70 in the MSP1 immune response. Rice protoplasts, co-expressing MSP1 and HSP70, showed a direct interaction between these two proteins in planta. Taken together, the results reported here highlight the pivotal role of HSP70 in MSP1-induced signaling and enhance our understanding of rice–M. oryzae interaction.