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CPSF30-L-mediated recognition of mRNA m 6 A modification controls alternative polyadenylation of nitrate signaling-related gene transcripts in Arabidopsis

N -methyladenosine (m A), a ubiquitous internal modification of eukaryotic mRNAs, plays a vital role in almost every aspect of mRNA metabolism. However, there is little evidence documenting the role of m A in regulating alternative polyadenylation (APA) in plants. APA is controlled by a large protei...

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Bibliographic Details
Published in:Molecular plant 2021-04, Vol.14 (4), p.688
Main Authors: Hou, Yifeng, Sun, Jing, Wu, Baixing, Gao, Yangyang, Nie, Hongbo, Nie, Zhentian, Quan, Shuxuan, Wang, Yong, Cao, Xiaofeng, Li, Sisi
Format: Article
Language:English
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Summary:N -methyladenosine (m A), a ubiquitous internal modification of eukaryotic mRNAs, plays a vital role in almost every aspect of mRNA metabolism. However, there is little evidence documenting the role of m A in regulating alternative polyadenylation (APA) in plants. APA is controlled by a large protein-RNA complex with many components, including CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR30 (CPSF30). In Arabidopsis, CPSF30 has two isoforms and the longer isoform (CPSF30-L) contains a YT512-B Homology (YTH) domain, which is unique to plants. In this study, we showed that CPSF30-L YTH domain binds to m A in vitro. In the cpsf30-2 mutant, the transcripts of many genes including several important nitrate signaling-related genes had shifts in polyadenylation sites that were correlated with m A peaks, indicating that these gene transcripts carrying m A tend to be regulated by APA. Wild-type CPSF30-L could rescue the defects in APA and nitrate metabolism in cpsf30-2, but m A-binding-defective mutants of CPSF30-L could not. Taken together, our results demonstrated that m A modification regulates APA in Arabidopsis and revealed that the m A reader CPSF30-L affects nitrate signaling by controlling APA, shedding new light on the roles of the m A modification during RNA 3'-end processing in nitrate metabolism.
ISSN:1752-9867