ArticleProceedings of the National Academy of Sciences of the United States of America2014
DEAD-box protein CYT-19 is activated by exposed helices in a group I intron RNA.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 28 citations in OpenAlex.
- Key Points to Consider When Studying RNA Remodeling by Proteins.Methods in molecular biology (Clifton, N.J.) · 2027Review
- High-resolution fleezers reveal duplex opening and stepwise assembly by an oligomer of the DEAD-box helicase Ded1p.Nature communications · 2025Article
- Moderate activity of RNA chaperone maximizes the yield of self-spliced pre-RNA in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- How to Kinetically Dissect an RNA Machine.Biochemistry · 2021Article
- Organellar Introns in Fungi, Algae, and Plants.Cells · 2021Review
- Rice OsRH58, a chloroplast DEAD-box RNA helicase, improves salt or drought stress tolerance in Arabidopsis by affecting chloroplast translation.BMC plant biology · 2019Article
- Distinct RNA-unwinding mechanisms of DEAD-box and DEAH-box RNA helicase proteins in remodeling structured RNAs and RNPs.Biochemical Society transactions · 2017Review
- The DEAD-Box Protein CYT-19 Uses Arginine Residues in Its C-Tail To Tether RNA Substrates.Biochemistry · 2017Article
- A DEAD-box RNA helicase promotes thermodynamic equilibration of kinetically trapped RNA structures in vivo.RNA (New York, N.Y.) · 2016Article
- Division of Labor in an Oligomer of the DEAD-Box RNA Helicase Ded1p.Molecular cell · 2015Article
- Melting of Duplex DNA in the Absence of ATP by the NS3 Helicase Domain through Specific Interaction with a Single-Strand/Double-Strand Junction.Biochemistry · 2015Article
- Unwinding the mechanisms of a DEAD-box RNA helicase in cancer.Journal of molecular biology · 2015Article
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- DEAD-box RNA helicase domains exhibit a continuum between complete functional independence and high thermodynamic coupling in nucleotide and RNA duplex recognition.Nucleic acids research · 2014Article
- Sisyphus observed: Unraveling the high ATP usage of an RNA chaperone.The Journal of biological chemistryArticle
- ATP utilization by a DEAD-box protein during refolding of a misfolded group I intron ribozyme.The Journal of biological chemistryArticle
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
DEAD-box proteins are nonprocessive RNA helicases and can function as RNA chaperones, but the mechanisms of their chaperone activity remain incompletely understood. The Neurospora crassa DEAD-box protein CYT-19 is a mitochondrial RNA chaperone that promotes group I intron splicing and has been shown to resolve misfolded group I intron structures, allowing them to refold. Building on previous results, here we use a series of tertiary contact mutants of the Tetrahymena group I intron ribozyme to demonstrate that the efficiency of CYT-19-mediated unfolding of the ribozyme is tightly linked to global RNA tertiary stability. Efficient unfolding of destabilized ribozyme variants is accompanied by increased ATPase activity of CYT-19, suggesting that destabilized ribozymes provide more productive interaction opportunities. The strongest ATPase stimulation occurs with a ribozyme that lacks all five tertiary contacts and does not form a compact structure, and small-angle X-ray scattering indicates that ATPase activity tracks with ribozyme compactness. Further, deletion of three helices that are prominently exposed in the folded structure decreases the ATPase stimulation by the folded ribozyme. Together, these results lead to a model in which CYT-19, and likely related DEAD-box proteins, rearranges complex RNA structures by preferentially interacting with and unwinding exposed RNA secondary structure. Importantly, this mechanism could bias DEAD-box proteins to act on misfolded RNAs and ribonucleoproteins, which are likely to be less compact and more dynamic than their native counterparts.
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