ArticleNucleic acids research2016
Structural basis for single-stranded RNA recognition and cleavage by C3PO.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Illustration of the variable 1D sequences but conserved 2D and 3D structures of different ncRNA nanostructures for tracking the evolution and origin of organisms.Non-coding RNA research · 2026Article
- Catalytic-state structure of Candidatus Hydrogenedentes Cas12b revealed by cryo-EM studies.Nucleic acids research · 2025Article
- Crystal structures and insights into precursor tRNA 5'-end processing by prokaryotic minimal protein-only RNase P.Nature communications · 2022Article
- Structural basis for guide RNA trimming by RNase D ribonuclease in Trypanosoma brucei.Nucleic acids research · 2021Article
- Translin: A multifunctional protein involved in nucleic acid metabolism.Journal of biosciences · 2019Review
- Structural insights into DNA degradation by human mitochondrial nuclease MGME1.Nucleic acids research · 2018Article
- Structural insights into Drosophila-C3PO complex assembly and 'Dynamic Side Port' model in substrate entry and release.Nucleic acids research · 2018Article
- Prosapip1-Dependent Synaptic Adaptations in the Nucleus Accumbens Drive Alcohol Intake, Seeking, and Reward.Neuron · 2017Article
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.