Structural insights reveal the specific recognition of meiRNA by the Mei2 protein
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In the fission yeastSchizosaccharomyces pombe,Mei2, an RNA-binding protein essential for entry into meiosis, regulates meiosis initiation. Mei2 bindstoa specific non-coding RNA species,meiRNA, and accumulates atsme2gene locus,which encodes meiRNA. Previous research has shownthatthe Mei2 C-terminalRNA recognition motif(RRM3)physically interacts with meiRNA 5′regionin vitroand stimulates meiosisin vivo. However, the underlying mechanism still remains elusive. We first employed anin vitrocrosslinking and immunoprecipitation sequencing (CLIP–seq)assay and demonstrated a preference for U-rich motifs of meiRNA by Mei2 RRM3.We then solved the crystal structures of Mei2 RRM3 in theapoform andcomplex with an 8mer RNAfragment,derived from meiRNA,as detected byin vitroCLIP–seq. These results provide structural insights into Mei2 RRM3–meiRNA complex and reveal that Mei2 RRM3 binds specificallytotheUUC(U)
sequence. Furthermore,a structure-based Mei2 mutation, Mei2F644Acauses defective karyogamy,suggesting an essential role ofthe RNA-binding ability of Mei2in regulating meiosis.
提供机构：
中国科学技术大学
创建时间：
2023-11-23
