Please use this identifier to cite or link to this item: https://scholarbank.nus.edu.sg/handle/10635/137683
Title: STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF SUBUNITS FROM TYPE III-A CRISPR/CAS COMPLEX, AND STRUCTURAL INSIGHTS INTO DROSOPHILA C3PO COMPLEX ASSEMBLY
Authors: MO XIAOBING
ORCID iD:   orcid.org/0000-0001-9580-6178
Keywords: RNA interference (RNAi), C3PO assembly, cryo-EM structure, X-Ray structure, CRISPR/Cas system, crRNA
Issue Date: 24-Aug-2017
Citation: MO XIAOBING (2017-08-24). STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF SUBUNITS FROM TYPE III-A CRISPR/CAS COMPLEX, AND STRUCTURAL INSIGHTS INTO DROSOPHILA C3PO COMPLEX ASSEMBLY. ScholarBank@NUS Repository.
Abstract: In Drosophila and human, Component 3 promoter of RISC (C3PO), a heteromeric complex, enhances RISC assembly and promotes RISC activity. Here, we report crystal and cryo-EM structures of full-length Drosophila C3PO (E126Q), an inactive C3PO mutant displaying much weaker RNA binding ability, at 2.1 Å and ~29 Å resolutions, as well as cryo-EM structure of full-length C3PO (WT) at ~12Å resolution. Notably, crystal structure of C3PO (E126Q) displays a half-barrel architecture consisting of two Trax/Translin heterodimers, whereas cryo-EM structures of C3PO (E126Q) and C3PO (WT) adopt a closed football-like shape with a hollow interior cavity. Remarkably, cryo-EM structure of C3PO (E126Q) contains a wide side port (25Å × 30Å) for RNA substrate entry and release. Here, we proposed a “Flip-flop” model that the alternative opening of side port at both side of C3PO during RNA substrate intake, digestion and release, and the intake of RNA substrate from one side port.
URI: http://scholarbank.nus.edu.sg/handle/10635/137683
Appears in Collections:Ph.D Theses (Open)

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