ArticleNucleic acids research2014
DEAD-box RNA helicase domains exhibit a continuum between complete functional independence and high thermodynamic coupling in nucleotide and RNA duplex recognition.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 39 citations in OpenAlex.
- Key Points to Consider When Studying RNA Remodeling by Proteins.Methods in molecular biology (Clifton, N.J.) · 2027Review
- DDX10 RNA Helicase: Structure, Function, and Oncogenic Roles Across Solid and Hematologic Tumors.Genes · 2026Review
- Role of DEAD/DEAH-box helicases in immunity, infection and cancers.Cell communication and signaling : CCS · 2025Review
- Long-range conformational changes in the nucleotide-bound states of the DEAD-box helicase Vasa.Biophysical journal · 2024Article
- The DEAD-box ATPase Dbp10/DDX54 initiates peptidyl transferase center formation during 60S ribosome biogenesis.Nature communications · 2024Article
- Structural basis for RNA-duplex unwinding by the DEAD-box helicase DbpA.RNA (New York, N.Y.) · 2023Article
- Structural basis for the activation of the DEAD-box RNA helicase DbpA by the nascent ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Specific Interaction of DDX6 with an RNA Hairpin in the 3' UTR of the Dengue Virus Genome Mediates GJournal of virology · 2021Article
- The DEAD-box protein family of RNA helicases: sentinels for a myriad of cellular functions with emerging roles in tumorigenesis.International journal of clinical oncology · 2021Review
- The Human RNA Helicase DDX21 Presents a Dimerization Interface Necessary for Helicase Activity.iScience · 2020Article
- TheRNA (New York, N.Y.) · 2020Article
- Dynamics of the DEAD-box ATPase Prp5 RecA-like domains provide a conformational switch during spliceosome assembly.Nucleic acids research · 2019Article
- Single-stranded regions modulate conformational dynamics and ATPase activity of eIF4A to optimize 5'-UTR unwinding.Nucleic acids research · 2019Article
- The DDX5/Dbp2 subfamily of DEAD-box RNA helicases.Wiley interdisciplinary reviews. RNA · 2019Review
- Distinct RNA-unwinding mechanisms of DEAD-box and DEAH-box RNA helicase proteins in remodeling structured RNAs and RNPs.Biochemical Society transactions · 2017Review
- Kinetics and Thermodynamics of DbpA Protein's C-Terminal Domain Interaction with RNA.ACS omega · 2017Article
- Biochemical Differences and Similarities between the DEAD-Box Helicase Orthologs DDX3X and Ded1p.Journal of molecular biology · 2017Article
- Characterization of the mammalian DEAD-box protein DDX5 reveals functional conservation withRNA (New York, N.Y.) · 2017Article
- Wnt signaling in triple-negative breast cancer.Oncogenesis · 2017Review
- Allosteric regulation of helicase core activities of the DEAD-box helicase YxiN by RNA binding to its RNA recognition motif.Nucleic acids research · 2017Article
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2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
DEAD-box helicases catalyze the non-processive unwinding of double-stranded RNA (dsRNA) at the expense of adenosine triphosphate (ATP) hydrolysis. Nucleotide and RNA binding and unwinding are mediated by the RecA domains of the helicase core, but their cooperation in these processes remains poorly understood. We therefore investigated dsRNA and nucleotide binding by the helicase cores and the isolated N- and C-terminal RecA domains (RecA_N, RecA_C) of the DEAD-box proteins Hera and YxiN by steady-state and time-resolved fluorescence methods. Both helicases bind nucleotides predominantly via RecA_N, in agreement with previous studies on Mss116, and with a universal, modular function of RecA_N in nucleotide recognition. In contrast, dsRNA recognition is different: Hera interacts with dsRNA in the absence of nucleotide, involving both RecA domains, whereas for YxiN neither RecA_N nor RecA_C binds dsRNA, and the complete core only interacts with dsRNA after nucleotide has been bound. DEAD-box proteins thus cover a continuum from complete functional independence of their domains, exemplified by Mss116, to various degrees of inter-domain cooperation in dsRNA binding. The different degrees of domain communication and of thermodynamic linkage between dsRNA and nucleotide binding have important implications on the mechanism of dsRNA unwinding, and may help direct RNA helicases to their respective cellular processes.
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