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Structural basis for single-stranded RNA recognition and cleavage by C3PO.

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  • Additional Information
    • Source:
      Publisher: Oxford University Press Country of Publication: England NLM ID: 0411011 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1362-4962 (Electronic) Linking ISSN: 03051048 NLM ISO Abbreviation: Nucleic Acids Res Subsets: MEDLINE
    • Publication Information:
      Publication: 1992- : Oxford : Oxford University Press
      Original Publication: London, Information Retrieval ltd.
    • Subject Terms:
      Models, Molecular* ; Molecular Conformation* ; RNA Cleavage*; Archaeal Proteins/*chemistry ; Archaeal Proteins/*metabolism ; RNA/*chemistry ; RNA-Binding Proteins/*chemistry ; RNA-Binding Proteins/*metabolism; Binding Sites ; Cations/chemistry ; Protein Binding ; RNA/metabolism ; Ribonucleases/chemistry ; Ribonucleases/metabolism ; Structure-Activity Relationship ; Substrate Specificity
    • Abstract:
      Translin and translin-associated factor-x are highly conserved in eukaroytes; they can form heteromeric complexes (known as C3POs) and participate in various nucleic acid metabolism pathways. In humans and Drosophila, C3POs cleave the fragmented siRNA passenger strands and facilitate the activation of RNA-induced silencing complex, the effector complex of RNA interference (RNAi). Here, we report three crystal structures of Nanoarchaeum equitans (Ne) C3PO. The apo-NeC3PO structure adopts an open form and unravels a potential substrates entryway for the first time. The NeC3PO:ssRNA and NeC3PO:ssDNA complexes fold like closed football with the substrates captured at the inner cavities. The NeC3PO:ssRNA structure represents the only catalytic form C3PO complex available to date; with mutagenesis and in vitro cleavage assays, the structure provides critical insights into the substrate binding and the two-cation-assisted catalytic mechanisms that are shared by eukaryotic C3POs. The work presented here further advances our understanding on the RNAi pathway.
      (© The Author(s) 2016. Published by Oxford University Press on behalf of Nucleic Acids Research.)
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    • Grant Information:
      R01 GM095881 United States GM NIGMS NIH HHS
    • Accession Number:
      0 (Archaeal Proteins)
      0 (Cations)
      0 (RNA-Binding Proteins)
      63231-63-0 (RNA)
      EC 3.1.- (Ribonucleases)
    • Publication Date:
      Date Created: 20160907 Date Completed: 20170606 Latest Revision: 20181113
    • Publication Date:
      20240829
    • Accession Number:
      PMC5100593
    • Accession Number:
      10.1093/nar/gkw776
    • Accession Number:
      27596600