ArticleRNA (New York, N.Y.)2023
Structural basis for RNA-duplex unwinding by the DEAD-box helicase DbpA.
Article in RNA (New York, N.Y.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Using Solution NMR to Study the RNA-Binding Properties and Molecular Mechanisms of the RNA Helicase DDX3X.Methods in molecular biology (Clifton, N.J.) · 2027Article
- 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
- Long-range conformational changes in the nucleotide-bound states of the DEAD-box helicase Vasa.Biophysical journal · 2024Article
- A role for the S4-domain containing protein YlmH in ribosome-associated quality control in Bacillus subtilis.Nucleic acids research · 2024Article
- Intrinsically disordered regions regulate RhlE RNA helicase functions in bacteria.Nucleic acids research · 2024Article
- 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
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Authors and funding
1 author.
Funding
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Abstract
DEAD-box RNA helicases are implicated in most aspects of RNA biology, where these enzymes unwind short RNA duplexes in an ATP-dependent manner. During the central step of the unwinding cycle, the two domains of the helicase core form a distinct closed conformation that destabilizes the RNA duplex, which ultimately leads to duplex melting. Despite the importance of this step for the unwinding process no high-resolution structures of this state are available. Here, I used nuclear magnetic resonance spectroscopy and X-ray crystallography to determine structures of the DEAD-box helicase DbpA in the closed conformation, complexed with substrate duplexes and single-stranded unwinding product. These structures reveal that DbpA initiates duplex unwinding by interacting with up to three base-paired nucleotides and a 5' single-stranded RNA duplex overhang. These high-resolution snapshots, together with biochemical assays, rationalize the destabilization of the RNA duplex and are integrated into a conclusive model of the unwinding process.
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