ArticleMolecular cell2007
Do DEAD-box proteins promote group II intron splicing without unwinding RNA?
Article in Molecular cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- Disassembly of unstable RNA structures by an E. coli DEAD-box chaperone accelerates ribosome assembly.Nucleic acids research · 2025Article
- 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
- The DEAD-box helicase Mss116 plays distinct roles in mitochondrial ribogenesis and mRNA-specific translation.Nucleic acids research · 2017Article
- A DEAD-box RNA helicase promotes thermodynamic equilibration of kinetically trapped RNA structures in vivo.RNA (New York, N.Y.) · 2016Article
- RNA-Seq profile of flavescence dorée phytoplasma in grapevine.BMC genomics · 2014Article
- Double-stranded DNA-dependent ATPase Irc3p is directly involved in mitochondrial genome maintenance.Nucleic acids research · 2014Article
- 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
- 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
- The brace for a growing scaffold: Mss116 protein promotes RNA folding by stabilizing an early assembly intermediate.Journal of molecular biology · 2012Article
- CRISPR immunity relies on the consecutive binding and degradation of negatively supercoiled invader DNA by Cascade and Cas3.Molecular cell · 2012Article
- ATP utilization and RNA conformational rearrangement by DEAD-box proteins.Annual review of biophysics · 2012Review
- 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
- 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
- Mechanism of Mss116 ATPase reveals functional diversity of DEAD-Box proteins.Journal of molecular biology · 2011Article
- Mne1 is a novel component of the mitochondrial splicing apparatus responsible for processing of a COX1 group I intron in yeast.The Journal of biological chemistry · 2011Article
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8 authors.
Funding
Abstract
The DEAD-box protein Mss116p promotes group II intron splicing in vivo and in vitro. Here we explore two hypotheses for how Mss116p promotes group II intron splicing: by using its RNA unwinding activity to act as an RNA chaperone or by stabilizing RNA folding intermediates. We show that an Mss116p mutant in helicase motif III (SAT/AAA), which was reported to stimulate splicing without unwinding RNA, retains ATP-dependent unwinding activity and promotes unfolding of a structured RNA. Its unwinding activity increases sharply with decreasing duplex length and correlates with group II intron splicing activity in quantitative assays. Additionally, we show that Mss116p can promote ATP-independent RNA unwinding, presumably via single-strand capture, also potentially contributing to DEAD-box protein RNA chaperone activity. Our findings favor the hypothesis that DEAD-box proteins function in group II intron splicing as in other processes by using their unwinding activity to act as RNA chaperones.
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