ArticleProceedings of the National Academy of Sciences of the United States of America2006
A DEAD-box protein alone promotes group II intron splicing and reverse splicing by acting as an RNA chaperone.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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50 citing papers in PubMed, 82 citations in OpenAlex.
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- Roles of Organellar RNA-Binding Proteins in Plant Growth, Development, and Abiotic Stress Responses.International journal of molecular sciences · 2020Review
- Mitochondrial Pentatricopeptide Repeat Protein, EMB2794, Plays a Pivotal Role in NADH Dehydrogenase Subunit nad2 mRNA Maturation in Arabidopsis thaliana.Plant & cell physiology · 2020Article
- Article
- Analysis of the Roles of the Arabidopsis nMAT2 and PMH2 Proteins Provided with New Insights into the Regulation of Group II Intron Splicing in Land-Plant Mitochondria.International journal of molecular sciences · 2017Article
- The DEAD-box helicase Mss116 plays distinct roles in mitochondrial ribogenesis and mRNA-specific translation.Nucleic acids research · 2017Article
- Emerging Roles of RNA-Binding Proteins in Plant Growth, Development, and Stress Responses.Molecules and cells · 2016Review
- A DEAD-box RNA helicase promotes thermodynamic equilibration of kinetically trapped RNA structures in vivo.RNA (New York, N.Y.) · 2016Article
- Mobile Bacterial Group II Introns at the Crux of Eukaryotic Evolution.Microbiology spectrum · 2015Review
- A nuclear-encoded chloroplast protein harboring a single CRM domain plays an important role in the Arabidopsis growth and stress response.BMC plant biology · 2014Article
- RNA helicase proteins as chaperones and remodelers.Annual review of biochemistry · 2014Review
- RNA catalytic activity as a probe of chaperone-mediated RNA folding.Methods in molecular biology (Clifton, N.J.) · 2014Article
- Toward a molecular understanding of RNA remodeling by DEAD-box proteins.RNA biology · 2013Review
- Mss116p: a DEAD-box protein facilitates RNA folding.RNA biology · 2013Review
- RNA catalysis as a probe for chaperone activity of DEAD-box helicases.Methods in enzymology · 2012Article
- High-throughput genetic identification of functionally important regions of the yeast DEAD-box protein Mss116p.Journal of molecular biology · 2011Article
- The Azoarcus group I intron ribozyme misfolds and is accelerated for refolding by ATP-dependent RNA chaperone proteins.The Journal of biological chemistry · 2011Article
- Ribozyme stability, exon skipping, and a potential role for RNA helicase in group I intron splicing by Coxiella burnetii.Journal of bacteriology · 2011Article
- ATP-dependent roles of the DEAD-box protein Mss116p in group II intron splicing in vitro and in vivo.Journal of molecular biology · 2011Article
- Group II introns: mobile ribozymes that invade DNA.Cold Spring Harbor perspectives in biology · 2011Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Group II intron RNAs self-splice in vitro but only at high salt and/or Mg2+ concentrations and have been thought to require proteins to stabilize their active structure for efficient splicing in vivo. Here, we show that a DEAD-box protein, CYT-19, can by itself promote the splicing and reverse splicing of the yeast aI5gamma and bI1 group II introns under near-physiological conditions by acting as an ATP-dependent RNA chaperone, whose continued presence is not required after RNA folding. Our results suggest that the folding of some group II introns may be limited by kinetic traps and that their active structures, once formed, do not require proteins or high Mg2+ concentrations for structural stabilization. Thus, during evolution, group II introns could have spliced and transposed by reverse splicing by using ubiquitous RNA chaperones before acquiring more specific protein partners to promote their splicing and mobility. More generally, our results provide additional evidence for the widespread role of RNA chaperones in folding cellular RNAs.
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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.