7EIO

Crystal Structure of Mei2 RRM3

Summary for 7EIO

• Entry DOI: 10.2210/pdb7eio/pdb
• Descriptor: Meiosis protein mei2, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: mei2, rrm, rna binding protein
• Biological source: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
• Total number of polymer chains: 2
• Total formula weight: 36095.01

Authors

Shen, S.Y.,Li, F.D. (deposition date: 2021-03-31, release date: 2022-04-06, Last modification date: 2024-05-29)

Primary citation

Shen, S.,Jian, Y.,Cai, Z.,Li, F.,Lv, M.,Liu, Y.,Wu, J.,Fu, C.,Shi, Y.
Structural insights reveal the specific recognition of meiRNA by the Mei2 protein.
J Mol Cell Biol, 14:-, 2022

PubMed Abstract: In the fission yeast Schizosaccharomyces pombe, Mei2, an RNA-binding protein essential for entry into meiosis, regulates meiosis initiation. Mei2 binds to a specific non-coding RNA species, meiRNA, and accumulates at the sme2 gene locus, which encodes meiRNA. Previous research has shown that the Mei2 C-terminal RNA recognition motif (RRM3) physically interacts with the meiRNA 5' region in vitro and stimulates meiosis in vivo. However, the underlying mechanisms still remain elusive. We first employed an in vitro crosslinking 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 the apo form and complex with an 8mer RNA fragment, derived from meiRNA, as detected by in vitro CLIP-seq. These results provide structural insights into the Mei2 RRM3-meiRNA complex and reveal that Mei2 RRM3 binds specifically to the UUC(U) sequence. Furthermore, a structure-based Mei2 mutation, Mei2F644A causes defective karyogamy, suggesting an essential role of the RNA-binding ability of Mei2 in regulating meiosis.

PubMed: 35512546
DOI: 10.1093/jmcb/mjac029

Experimental method

X-RAY DIFFRACTION (1.895 Å)