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Publication : Structure of C3PO and mechanism of human RISC activation.

First Author  Ye X Year  2011
Journal  Nat Struct Mol Biol Volume  18
Issue  6 Pages  650-7
PubMed ID  21552258 Mgi Jnum  J:320273
Mgi Id  MGI:6870974 Doi  10.1038/nsmb.2032
Citation  Ye X, et al. (2011) Structure of C3PO and mechanism of human RISC activation. Nat Struct Mol Biol 18(6):650-7
abstractText  Assembly of the RNA-induced silencing complex (RISC) consists of loading duplex (guide-passenger) siRNA onto Argonaute (Ago2) and removing the passenger strand. Ago2 contributes critically to RISC activation by nicking the passenger strand. Here we reconstituted duplex siRNA-initiated RISC activity using recombinant human Ago2 (hAgo2) and C3PO, indicating that C3PO has a critical role in hAgo2-RISC activation. Consistently, genetic depletion of C3PO compromised RNA silencing in mammalian cells. We determined the crystal structure of hC3PO, which reveals an asymmetric octamer barrel consisting of six translin and two TRAX subunits. This asymmetric assembly is critical for the function of C3PO as an endonuclease that cleaves RNA at the interior surface. The current work supports a Dicer-independent mechanism for human RISC activation, in which Ago2 directly binds duplex siRNA and nicks the passenger strand, and then C3PO activates RISC by degrading the Ago2-nicked passenger strand.
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