ArticleRNA (New York, N.Y.)2017
Structure of the DEAH/RHA ATPase Prp43p bound to RNA implicates a pair of hairpins and motif Va in translocation along RNA.
Article in RNA (New York, N.Y.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 53 citations in OpenAlex.
- Asymmetric dimeric assembly of Suv3 helicase facilitates processive RNA unwinding.Nature communications · 2026Article
- Annotation and functional prediction of RNA helicases inIMA fungus · 2025Review
- Impact of bound ssRNA length on allostery in the Dengue Virus NS3 helicase.Nucleic acids research · 2023Article
- Conformational dynamics of the RNA binding channel regulates loading and translocation of the DEAH-box helicase Prp43.Nucleic acids research · 2023Article
- Superfamily II helicases: the potential therapeutic target for cardiovascular diseases.Frontiers in cardiovascular medicine · 2023Review
- Regulation of the DEAH/RHA helicase Prp43 by the G-patch factor Pfa1.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Measuring the impact of cofactors on RNA helicase activities.Methods (San Diego, Calif.) · 2022Article
- Action and function of helicases on RNA G-quadruplexes.Methods (San Diego, Calif.) · 2022Review
- Article
- RNA folding and functions of RNA helicases in ribosome biogenesis.RNA biology · 2022Review
- Large-scale ratcheting in a bacterial DEAH/RHA-type RNA helicase that modulates antibiotics susceptibility.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Mtr4 RNA helicase structures and interactions.Biological chemistry · 2021Review
- The structure of Prp2 bound to RNA and ADP-BeFActa crystallographica. Section D, Structural biology · 2021Article
- The G-patch activators Pfa1 and PINX1 exhibit different modes of interaction with the Prp43 RNA helicase.RNA biology · 2021Article
- psiCLIP reveals dynamic RNA binding by DEAH-box helicases before and after exon ligation.Nature communications · 2021Article
- DEAH-Box RNA Helicases in Pre-mRNA Splicing.Trends in biochemical sciences · 2021Review
- Auxiliary domains of the HrpB bacterial DExH-box helicase shape its RNA preferences.RNA biology · 2020Article
- Structural basis for DEAH-helicase activation by G-patch proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Function of Auxiliary Domains of the DEAH/RHA Helicase DHX36 in RNA Remodeling.Journal of molecular biology · 2020Article
- Splicing factor DHX15 affects tp53 and mdm2 expression via alternate splicing and promoter usage.Human molecular genetics · 2019Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Three families of nucleic acid-dependent ATPases (DEAH/RHA, Ski2-like, and NS3/NPH-II), termed the DExH ATPases, are thought to execute myriad functions by processive, ATP-dependent, 3' to 5' translocation along single-stranded nucleic acid. While the mechanism of translocation of the viral NS3/NPH-II family has been studied extensively, it has not been clear if or how the principles that have emerged for this family extend to the other two families. Here we report the crystal structure of the yeast DEAH/RHA family ATPase Prp43p, which functions in splicing and ribosome biogenesis, in complex with poly-uracil and a nonhydrolyzable ATP analog. The structure reveals a conserved DEAH/RHA-specific variation of motif Ib within the RecA1 domain of the catalytic core, in which the motif elongates as a β-hairpin that bookends the 3' end of a central RNA stack, a function that in the viral and Ski-2 families is performed by an auxiliary domain. Supporting a fundamental role in translocation, mutations in this hairpin abolished helicase activity without affecting RNA binding or ATPase activity. While the structure reveals differences with viral ATPases in the RecA1 domain, our structure demonstrates striking similarities with viral ATPases in the RecA2 domain of the catalytic core, including both a prominent β-hairpin that bookends the 5' end of the RNA stack and a dynamic motif Va that is implicated in mediating translocation. Our crystal structure, genetic, and biochemical experiments, as well as comparisons with other DExH ATPases, support a generalized mechanism for the DExH class of helicases involving a pair of bookends that inchworm along RNA.
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