ArticleNucleic acids research2009
A novel dimerization motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibility.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 57 citations in OpenAlex.
- GeoPep: A Geometry-Aware Masked Language Model for Protein-Peptide Binding Site Prediction.Journal of chemical information and modeling · 2026Article
- Asymmetric dimeric assembly of Suv3 helicase facilitates processive RNA unwinding.Nature communications · 2026Article
- Tho1 and MOS11 promote nucleic acid double-strand unwinding by facilitating DEAD-box helicase oligomerization.Nucleic acids research · 2026Article
- 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
- Measuring the impact of cofactors on RNA helicase activities.Methods (San Diego, Calif.) · 2022Article
- Degron-mediated proteolysis of CrhR-like DEAD-box RNA helicases in cyanobacteria.The Journal of biological chemistry · 2022Article
- Roles of the C-Terminal Amino Acids of Non-Hexameric Helicases: Insights fromInternational journal of molecular sciences · 2021Review
- The Human RNA Helicase DDX21 Presents a Dimerization Interface Necessary for Helicase Activity.iScience · 2020Article
- Functions of Gle1 are governed by two distinct modes of self-association.The Journal of biological chemistry · 2020Article
- TheRNA (New York, N.Y.) · 2020Article
- DNA-Unwinding Dynamics of Escherichia coli UvrD Lacking the C-Terminal 40 Amino Acids.Biophysical journal · 2020Article
- SMN complex member Gemin3 self-interacts and has a functional relationship with ALS-linked proteins TDP-43, FUS and Sod1.Scientific reports · 2019Article
- The DEAD-Box RNA Helicases ofFrontiers in microbiology · 2018Article
- Unzippers, resolvers and sensors: a structural and functional biochemistry tale of RNA helicases.International journal of molecular sciences · 2015Review
- Measuring helicase inhibition of the DEAD-box protein Dbp2 by Yra1.Methods in molecular biology (Clifton, N.J.) · 2015Article
- Genome-wide analysis of the RNA helicase gene family in Gossypium raimondii.International journal of molecular sciences · 2014Article
- Intra- and intermolecular regulatory interactions in Upf1, the RNA helicase central to nonsense-mediated mRNA decay in yeast.Molecular and cellular biology · 2013Article
- DEAD-box helicases as integrators of RNA, nucleotide and protein binding.Biochimica et biophysica acta · 2013Review
- Recognition of two distinct elements in the RNA substrate by the RNA-binding domain of the T. thermophilus DEAD box helicase Hera.Nucleic acids research · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DEAD box helicases are involved in nearly all aspects of RNA metabolism. They share a common helicase core, and may comprise additional domains that contribute to RNA binding. The Thermus thermophilus helicase Hera is the first dimeric DEAD box helicase. Crystal structures of Hera fragments reveal a bipartite C-terminal domain with a novel dimerization motif and an RNA-binding module. We provide a first glimpse on the additional RNA-binding module outside the Hera helicase core. The dimerization and RNA-binding domains are connected to the C-terminal RecA domain by a hinge region that confers exceptional flexibility onto the helicase, allowing for different juxtapositions of the RecA-domains in the dimer. Combination of the previously determined N-terminal Hera structure with the C-terminal Hera structures allows generation of a model for the entire Hera dimer, where two helicase cores can work in conjunction on large RNA substrates.
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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.