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TitleStructural Basis for pri-miRNA Recognition by Drosha.
Journal, issue, pagesMol Cell, Vol. 78, Issue 3, Page 423-433.e5, Year 2020
Publish dateMay 7, 2020
AuthorsWenxing Jin / Jia Wang / Chao-Pei Liu / Hong-Wei Wang / Rui-Ming Xu /
PubMed AbstractA commencing and critical step in miRNA biogenesis involves processing of pri-miRNAs in the nucleus by Microprocessor. An important, but not completely understood, question is how Drosha, the ...A commencing and critical step in miRNA biogenesis involves processing of pri-miRNAs in the nucleus by Microprocessor. An important, but not completely understood, question is how Drosha, the catalytic subunit of Microprocessor, binds pri-miRNAs and correctly specifies cleavage sites. Here we report the cryoelectron microscopy structures of the Drosha-DGCR8 complex with and without a pri-miRNA. The RNA-bound structure provides direct visualization of the tertiary structure of pri-miRNA and shows that a helix hairpin in the extended PAZ domain and the mobile basic (MB) helix in the RNase IIIa domain of Drosha coordinate to recognize the single-stranded to double-stranded junction of RNA, whereas the dsRNA binding domain makes extensive contacts with the RNA stem. Furthermore, the RNA-free structure reveals an autoinhibitory conformation of the PAZ helix hairpin. These findings provide mechanistic insights into pri-miRNA cleavage site selection and conformational dynamics governing pri-miRNA recognition by the catalytic component of Microprocessor.
External linksMol Cell / PubMed:32220645
MethodsEM (single particle)
Resolution3.9 - 4.2 Å
Structure data

30005

6lxd

EMDB-30005: pri-miRNA bound DROSHA-DGCR8 complex
PDB-6lxd: Pri-miRNA bound DROSHA-DGCR8 complex
Method: EM (single particle) / Resolution: 3.9 Å

30006

6lxe

EMDB-30006, PDB-6lxe:
DROSHA-DGCR8 complex
Method: EM (single particle) / Resolution: 4.2 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsHYDROLASE/RNA BINDING PROTEIN/RNA / Ribonuclease / RNA BINDING PROTEIN / HYDROLASE-RNA BINDING PROTEIN-RNA complex / HYDROLASE/RNA BINDING PROTEIN / HYDROLASE-RNA BINDING PROTEIN complex

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