ArticleNature2012
Structural basis for RNA-duplex recognition and unwinding by the DEAD-box helicase Mss116p.
Article in Nature, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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Who cites it
73 citing papers in PubMed.
- Global Identification of RNA Helicase Substrates from Large Nucleic Acid Sequence Libraries Using Helicase-SELEX.Methods in molecular biology (Clifton, N.J.) · 2027Article
- DDX17 and viral infection.Virulence · 2026Review
- Redesign of energetically frustrated regions rescues function in defective T4 clamp loaders.Molecular biology and evolution · 2026Article
- DDX3X induces mesenchymal transition of endothelial cells by disrupting BMPR2 signaling.FEBS open bio · 2026Article
- DDX24 modulates angiogenesis by promoting CCR4-NOT complex-dependent mRNA decay.Nucleic acids research · 2026Article
- DDX10 RNA Helicase: Structure, Function, and Oncogenic Roles Across Solid and Hematologic Tumors.Genes · 2026Review
- Competitive binding between DDX21 and SIRT7 enhances NAT10-mediated acCell death & disease · 2025Article
- Inter-domain communication in the dimeric DEAD-box helicase Hera from T. thermophilus and implications for the mechanism of RNA unwinding.Nucleic acids research · 2025Article
- High-resolution fleezers reveal duplex opening and stepwise assembly by an oligomer of the DEAD-box helicase Ded1p.Nature communications · 2025Article
- Long-range conformational changes in the nucleotide-bound states of the DEAD-box helicase Vasa.Biophysical journal · 2024Article
- Critical Cellular Functions and Mechanisms of Action of the RNA Helicase UAP56.Journal of molecular biology · 2024Review
- NMR characterization of RNA binding property of the DEAD-box RNA helicase DDX3X and its implications for helicase activity.Nature communications · 2024Article
- The DEAD-box ATPase Dbp10/DDX54 initiates peptidyl transferase center formation during 60S ribosome biogenesis.Nature communications · 2024Article
- Autoinhibition of a clamp-loader ATPase revealed by deep mutagenesis and cryo-EM.Nature structural & molecular biology · 2024Article
- Cellular functions of eukaryotic RNA helicases and their links to human diseases.Nature reviews. Molecular cell biology · 2023Review
- Structural basis for RNA-duplex unwinding by the DEAD-box helicase DbpA.RNA (New York, N.Y.) · 2023Article
- Concurrent remodelling of nucleolar 60S subunit precursors by the Rea1 ATPase and Spb4 RNA helicase.eLife · 2023Article
- The DEAD-box protein Dbp6 is an ATPase and RNA annealase interacting with the peptidyl transferase center (PTC) of the ribosome.Nucleic acids research · 2023Article
- Sequence-specific remodeling of a topologically complex RNP substrate by Spb4.Nature structural & molecular biology · 2022Article
- Article
13 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors.
Funding
Abstract
DEAD-box proteins are the largest family of nucleic acid helicases, and are crucial to RNA metabolism throughout all domains of life. They contain a conserved 'helicase core' of two RecA-like domains (domains (D)1 and D2), which uses ATP to catalyse the unwinding of short RNA duplexes by non-processive, local strand separation. This mode of action differs from that of translocating helicases and allows DEAD-box proteins to remodel large RNAs and RNA-protein complexes without globally disrupting RNA structure. However, the structural basis for this distinctive mode of RNA unwinding remains unclear. Here, structural, biochemical and genetic analyses of the yeast DEAD-box protein Mss116p indicate that the helicase core domains have modular functions that enable a novel mechanism for RNA-duplex recognition and unwinding. By investigating D1 and D2 individually and together, we find that D1 acts as an ATP-binding domain and D2 functions as an RNA-duplex recognition domain. D2 contains a nucleic-acid-binding pocket that is formed by conserved DEAD-box protein sequence motifs and accommodates A-form but not B-form duplexes, providing a basis for RNA substrate specificity. Upon a conformational change in which the two core domains join to form a 'closed state' with an ATPase active site, conserved motifs in D1 promote the unwinding of duplex substrates bound to D2 by excluding one RNA strand and bending the other. Our results provide a comprehensive structural model for how DEAD-box proteins recognize and unwind RNA duplexes. This model explains key features of DEAD-box protein function and affords a new perspective on how the evolutionarily related cores of other RNA and DNA helicases diverged to use different mechanisms.
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