ArticleJournal of molecular biology2011
ATP-dependent roles of the DEAD-box protein Mss116p in group II intron splicing in vitro and in vivo.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 31 citations in OpenAlex.
- 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
- Assembly factors chaperone ribosomal RNA folding by isolating helical junctions that are prone to misfolding.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Probing Transcriptome-Wide RNA Structural Changes Dependent on the DEAD-box Helicase Dbp2.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Genome-Wide Discovery of DEAD-Box RNA Helicase Targets Reveals RNA Structural Remodeling in Transcription Termination.Genetics · 2019Article
- The DDX5/Dbp2 subfamily of DEAD-box RNA helicases.Wiley interdisciplinary reviews. RNA · 2019Review
- Molecular chaperones maximize the native state yield on biological times by driving substrates out of equilibrium.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- 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
- Article
- DEAD-box protein CYT-19 is activated by exposed helices in a group I intron RNA.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Yeast DEAD box protein Mss116p is a transcription elongation factor that modulates the activity of mitochondrial RNA polymerase.Molecular and cellular 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
- Mss116p: a DEAD-box protein facilitates RNA folding.RNA biology · 2013Review
- Toward a molecular understanding of RNA remodeling by DEAD-box proteins.RNA biology · 2013Review
- Structural basis for RNA-duplex recognition and unwinding by the DEAD-box helicase Mss116p.Nature · 2012Article
- The brace for a growing scaffold: Mss116 protein promotes RNA folding by stabilizing an early assembly intermediate.Journal of molecular biology · 2012Article
- 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
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The yeast DEAD-box protein Mss116p functions as a general RNA chaperone in splicing mitochondrial group I and group II introns. For most of its functions, Mss116p is thought to use ATP-dependent RNA unwinding to facilitate RNA structural transitions, but it has been suggested to assist in the folding of one group II intron (aI5γ) primarily by stabilizing a folding intermediate. Here we compare three aI5γ constructs: one with long exons, one with short exons, and a ribozyme construct lacking exons. The long exons result in slower splicing, suggesting that they misfold and/or stabilize nonnative intronic structures. Nevertheless, Mss116p acceleration of all three constructs depends on ATP and is inhibited by mutations that compromise RNA unwinding, suggesting similar mechanisms. Results of splicing assays and a new two-stage assay that separates ribozyme folding and catalysis indicate that maximal folding of all three constructs by Mss116p requires ATP-dependent RNA unwinding. ATP-independent activation is appreciable for only a subpopulation of the minimal ribozyme construct and not for constructs containing exons. As expected for a general RNA chaperone, Mss116p can also disrupt the native ribozyme, which can refold after Mss116p removal. Finally, using yeast strains with mitochondrial DNA containing only the single intron aI5γ, we show that Mss116p mutants promote splicing in vivo to degrees that correlate with their residual ATP-dependent RNA-unwinding activities. Together, our results indicate that, although DEAD-box proteins play multiple roles in RNA folding, the physiological function of Mss116p in aI5γ splicing includes a requirement for ATP-dependent local unfolding, allowing the conversion of nonfunctional RNA structure into functional RNA structure.
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