ArticleProceedings of the National Academy of Sciences of the United States of America2002
Recruitment of intron-encoded and co-opted proteins in splicing of the bI3 group I intron RNA.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 48 citations in OpenAlex.
- Refining Mitochondrial Intron Classification With ERPIN: Identification Based on Conservation of Sequence Plus Secondary Structure Motifs.Frontiers in microbiology · 2022Article
- Review
- Bacterial group I introns: mobile RNA catalysts.Mobile DNA · 2014Article
- On the importance of cotranscriptional RNA structure formation.RNA (New York, N.Y.) · 2013Review
- Mss116p: a DEAD-box protein facilitates RNA folding.RNA biology · 2013Review
- Article
- Exploring RNA structural codes with SHAPE chemistry.Accounts of chemical research · 2011Article
- Recurrent insertion of 5'-terminal nucleotides and loss of the branchpoint motif in lineages of group II introns inserted in mitochondrial preribosomal RNAs.RNA (New York, N.Y.) · 2011Article
- Evolutionary dynamics of the mS952 intron: a novel mitochondrial group II intron encoding a LAGLIDADG homing endonuclease gene.Journal of molecular evolution · 2011Article
- Evolution of introns in the archaeal world.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- A group II intron encodes a functional LAGLIDADG homing endonuclease and self-splices under moderate temperature and ionic conditions.RNA (New York, N.Y.) · 2010Article
- Nonhierarchical ribonucleoprotein assembly suggests a strain-propagation model for protein-facilitated RNA folding.Biochemistry · 2010Article
- Splicing of yeast aI5beta group I intron requires SUV3 to recycle MRS1 via mitochondrial degradosome-promoted decay of excised intron ribonucleoprotein (RNP).The Journal of biological chemistry · 2010Article
- The Mrs1 splicing factor binds the bI3 group I intron at each of two tetraloop-receptor motifs.PloS one · 2010Article
- Leucyl-tRNA synthetase-dependent and -independent activation of a group I intron.The Journal of biological chemistry · 2009Article
- High-throughput SHAPE and hydroxyl radical analysis of RNA structure and ribonucleoprotein assembly.Methods in enzymology · 2009Article
- A DExH/D-box protein coordinates the two steps of splicing in a group I intron.Journal of molecular biology · 2008Article
- SHAPE analysis of long-range interactions reveals extensive and thermodynamically preferred misfolding in a fragile group I intron RNA.Biochemistry · 2008Article
- A C-terminal fragment of an intron-encoded maturase is sufficient for promoting group I intron splicing.RNA (New York, N.Y.) · 2005Article
- The splicing of yeast mitochondrial group I and group II introns requires a DEAD-box protein with RNA chaperone function.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Detectable splicing by the Saccharomyces cerevisiae mitochondrial bI3 group I intron RNA in vitro is shown to require both an intron-encoded protein, the bI3 maturase, and the nuclear-encoded protein, Mrs1. Both proteins bind independently to the bI3 RNA. The bI3 maturase binds as a monomer, whereas Mrs1 is a dimer in solution that assembles as two dimers, cooperatively, on the RNA. The active six-subunit complex has a molecular mass of 420 kDa, splices with a k(cat) of 0.3 min(-1), and binds the guanosine nucleophile with an affinity comparable to other group I introns. The functional bI3 maturase domain is translated from within the RNA that encodes the intron, has evolved a high-affinity RNA-binding activity, and is a member of the LAGLIDADG family of DNA endonucleases, but appears to have lost DNA cleavage activity. Mrs1 is a divergent member of the RNase H fold superfamily of dimeric DNA junction-resolving enzymes that also appears to have lost its nuclease activity and now functions as a tetramer in RNA binding. Thus, the bI3 ribonucleoprotein is the product of a process in which a once-catalytically active RNA now obligatorily requires two facilitating protein cofactors, both of which are compromised in their original functions.
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