ArticleJournal of molecular biology2010
Protein-facilitated folding of group II intron ribozymes.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Elucidating structure-function relationships in the mammalian nucleolus.Nature reviews. Molecular cell biology · 2026Review
- LncRNA SChLAP1 Promotes Cancer Cell Proliferation and Invasion Via Its Distinct Structural Domains and Conserved Regions.Journal of molecular biology · 2025Article
- Disassembly of unstable RNA structures by an E. coli DEAD-box chaperone accelerates ribosome assembly.Nucleic acids research · 2025Article
- Long-range conformational changes in the nucleotide-bound states of the DEAD-box helicase Vasa.Biophysical journal · 2024Article
- Review
- Functions of PPR Proteins in Plant Growth and Development.International journal of molecular sciences · 2021Review
- Rerouting of ribosomal proteins into splicing in plant organelles.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Sequencing and Structure Probing of Long RNAs Using MarathonRT: A Next-Generation Reverse Transcriptase.Journal of molecular biology · 2020Article
- 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
- Review
- A structure-based mechanism for tRNA and retroviral RNA remodelling during primer annealing.Nature · 2014Article
- RNA helicase proteins as chaperones and remodelers.Annual review of biochemistry · 2014Review
- Group II intron splicing factors in plant mitochondria.Frontiers in plant science · 2014Review
- The DEAD-box protein Dbp2 functions with the RNA-binding protein Yra1 to promote mRNP assembly.Journal of molecular biology · 2013Article
- The structural stabilization of the κ three-way junction by Mg(II) represents the first step in the folding of a group II intron.Nucleic acids research · 2013Article
- 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
- The brace for a growing scaffold: Mss116 protein promotes RNA folding by stabilizing an early assembly intermediate.Journal of molecular biology · 2012Article
- Selective forces for the origin of spliceosomes.Journal of molecular evolution · 2012Article
- RNA catalysis as a probe for chaperone activity of DEAD-box helicases.Methods in enzymology · 2012Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Multiple studies hypothesize that DEAD-box proteins facilitate folding of the ai5gamma group II intron. However, these conclusions are generally inferred from splicing kinetics, and not from direct monitoring of DEAD-box protein-facilitated folding of the intron. Using native gel electrophoresis and dimethyl sulfate structural probing, we monitored Mss-116-facilitated folding of ai5gamma intron ribozymes and a catalytically active self-splicing RNA containing full-length intron and short exons. We found that the protein directly stimulates folding of these RNAs by accelerating formation of the compact near-native state. This process occurs in an ATP-independent manner, although ATP is required for the protein turnover. As Mss 116 binds RNA nonspecifically, most binding events do not result in the formation of the compact state, and ATP is required for the protein to dissociate from such nonproductive complexes and rebind the unfolded RNA. Results obtained from experiments at different concentrations of magnesium ions suggest that Mss 116 stimulates folding of ai5gamma ribozymes by promoting the formation of unstable folding intermediates, which is then followed by a cascade of folding events resulting in the formation of the compact near-native state. Dimethyl sulfate probing results suggest that the compact state formed in the presence of the protein is identical to the near-native state formed more slowly in its absence. Our results also indicate that Mss 116 does not stabilize the native state of the ribozyme, but that such stabilization results from binding of attached exons.
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