m6A modification plays an integral role in mRNA stability and translation during pattern- triggered immunity

• 成果类型: Article
• 署名作者: Chen, Tianyuan; Greene, George H.; Motley, Jonathan; Mwimba, Musoki; Luo, Guan - Zheng; Xu, Guoyong; Karapetyan, Sargis; Xiang, Yezi; Liu, Chang; He, Chuan; Dong, Xinnian
• 署名单位: Howard Hughes Medical Institute; Duke University; Duke University; Howard Hughes Medical Institute; University of Chicago; University of Chicago; Wuhan University
• 刊物名称: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
• ISSN/ISSBN: 0027-15359
• DOI: 10.1073/pnas.2411100121
• 发表日期: 2024-08-13
• 关键词: ythdf proteins; n-6-methyladenosine; resistance

摘要

Plants employ distinct mechanisms to respond to environmental changes. Modification mRNA by N 6- methyladenosine (m6A), known to affect the fate of mRNA, maybe one such mechanism to reprogram mRNA processing and translatability upon stress. However, is difficult to distinguish a direct role from a pleiotropic effect for this modification due its prevalence in RNA. Through characterization of the transient knockdown- mutants m6A writer components and mutants of specific m6A readers,we demonstrate the essential role that m6A plays in basal resistance and pattern- triggered immunity (PTI). A global m6A profiling of mock and PTI- induced Arabidopsis plants as well as formaldehyde fixation and cross- linking immunoprecipitation- sequencing of the m6A reader, EVOLUTIONARILY CONSERVED C- TERMINAL REGION2 (ECT2) showed that while dynamic changes in m6A modification and binding by ECT2 were detected upon PTI induction, most of the m6A sites and their association with ECT2 remained static. Interestingly, RNA degradation assay identified a dual role of m6A in stabilizing the overall transcriptome while facilitating rapid turnover of immune- induced mRNAs during PTI. Moreover, polysome profiling showed that m6A enhances immune- associated translation by binding to the ECT2/3/4 readers. We propose that m6A plays a positive role in plant immunity by destabilizing defense mRNAs while enhancing their translation efficiency to create a transient surge the production of defense proteins.