An mA methyltransferase confers host resistance by degrading viral proteins through ubiquitination.

Nat Commun

State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Key Laboratory of Biotechnology in Plant Protection of MARA, Key Laboratory of Green Plant Protection of Zhejiang Province, Institute of Plant Virology, Ningbo University, Ningbo, China. nather2

Published: May 2025


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Article Abstract

Posttranscriptional and posttranslational modifications play crucial roles in plant immunity. However, how plants fine-tune such modifications to activate antiviral immunity remains unknown. Here, we report that the mA methyltransferase TaHAKAI is utilized by wheat yellow mosaic virus (WYMV) to increase viral genomic mA modification and promote viral replication. However, TaHAKAI also functions as an E3 ligase that targets the viral RNA silencing suppressor P2 for degradation and inhibits viral infection. A major allele of TaHAKAI in a susceptible cultivar exhibited reduced E3 ligase activity but not mA methyltransferase activity, promoting viral infection. Interestingly, TaHAKAI attenuates the stability of TaWPS1 (Wheat paired spikelets 1, WPS1) mRNA, the negative regulator of spike development, which might increase panicle length and spikelet number by modulating its mA modification. Our study reveals a mechanism for balancing disease resistance and yield by fine-tuning mA modification and ubiquitination.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC12102378PMC
http://dx.doi.org/10.1038/s41467-025-60199-1DOI Listing

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