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Structural basis of microRNA biogenesis by Dicer-1 and its partner protein Loqs-PB

K. Jouravleva, D. Golovenko, G. Demo, RC. Dutcher, TMT. Hall, PD. Zamore, AA. Korostelev

. 2022 ; 82 (21) : 4049-4063.e6. [pub] 20220930

Language English Country United States

Document type Journal Article, Research Support, N.I.H., Intramural, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't

Persistent link   https://www.medvik.cz/link/bmc22032748

Grant support
R35 GM127094 NIGMS NIH HHS - United States
R35 GM136275 NIGMS NIH HHS - United States
ZIA ES050165 Intramural NIH HHS - United States

In animals and plants, Dicer enzymes collaborate with double-stranded RNA-binding domain (dsRBD) proteins to convert precursor-microRNAs (pre-miRNAs) into miRNA duplexes. We report six cryo-EM structures of Drosophila Dicer-1 that show how Dicer-1 and its partner Loqs-PB cooperate (1) before binding pre-miRNA, (2) after binding and in a catalytically competent state, (3) after nicking one arm of the pre-miRNA, and (4) following complete dicing and initial product release. Our reconstructions suggest that pre-miRNA binds a rare, open conformation of the Dicer-1⋅Loqs-PB heterodimer. The Dicer-1 dsRBD and three Loqs-PB dsRBDs form a tight belt around the pre-miRNA, distorting the RNA helix to place the scissile phosphodiester bonds in the RNase III active sites. Pre-miRNA cleavage shifts the dsRBDs and partially closes Dicer-1, which may promote product release. Our data suggest a model for how the Dicer-1⋅Loqs-PB complex affects a complete cycle of pre-miRNA recognition, stepwise endonuclease cleavage, and product release.

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