ArticleBiochemistry2010
Nonhierarchical ribonucleoprotein assembly suggests a strain-propagation model for protein-facilitated RNA folding.
Article in Biochemistry, 2010. 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 24 citations in OpenAlex.
- Fuzzy RNA recognition by the Trypanosoma brucei editosome.Nucleic acids research · 2022Article
- Protein cofactors and substrate influence Mg2+-dependent structural changes in the catalytic RNA of archaeal RNase P.Nucleic acids research · 2021Article
- A systemic identification approach for primary transcription start site of Arabidopsis miRNAs from multidimensional omics data.Functional & integrative genomics · 2017Article
- Selective 2'-hydroxyl acylation analyzed by primer extension and mutational profiling (SHAPE-MaP) for direct, versatile and accurate RNA structure analysis.Nature protocols · 2015Article
- Single-molecule studies of riboswitch folding.Biochimica et biophysica acta · 2014Review
- Magnesium-dependent folding of a picornavirus IRES element modulates RNA conformation and eIF4G interaction.The FEBS journal · 2014Article
- Molecular crowders and cosolutes promote folding cooperativity of RNA under physiological ionic conditions.RNA (New York, N.Y.) · 2014Article
- Hierarchy of RNA functional dynamics.Annual review of biochemistry · 2014Review
- Tackling structures of long noncoding RNAs.International journal of molecular sciences · 2013Review
- Gemin5 promotes IRES interaction and translation control through its C-terminal region.Nucleic acids research · 2013Article
- Fingerprinting noncanonical and tertiary RNA structures by differential SHAPE reactivity.Journal of the American Chemical Society · 2012Article
- Assembly of the five-way junction in the ribosomal small subunit using hybrid MD-Gō simulations.The journal of physical chemistry. B · 2012Article
- Review
- Exploring RNA structural codes with SHAPE chemistry.Accounts of chemical research · 2011Article
- Selective 2'-hydroxyl acylation analyzed by protection from exoribonuclease (RNase-detected SHAPE) for direct analysis of covalent adducts and of nucleotide flexibility in RNA.Nature protocols · 2011Article
- Slow formation of stable complexes during coincubation of minimal rRNA and ribosomal protein S4.Journal of molecular biology · 2011Article
- Transient RNA-protein interactions in RNA folding.The FEBS journal · 2011Review
- 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
- Mechanisms of StpA-mediated RNA remodeling.RNA biologyReview
- RNA structural analysis by evolving SHAPE chemistry.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Proteins play diverse and critical roles in cellular ribonucleoproteins (RNPs) including promoting formation of and stabilizing active RNA conformations. Yet, the conformational changes required to convert large RNAs into active RNPs have proven difficult to characterize fully. Here we use high-resolution approaches to monitor both local nucleotide flexibility and solvent accessibility for nearly all nucleotides in the bI3 group I intron RNP in four assembly states: the free RNA, maturase-bound RNA, Mrs1-bound RNA, and the complete six-component holocomplex. The free RNA is misfolded relative to the secondary structure required for splicing. The maturase and Mrs1 proteins each stabilized long-range tertiary interactions, but neither protein alone induced folding into the functional secondary structure. In contrast, simultaneous binding by both proteins results in large secondary structure rearrangements in the RNA and yielded the catalytically active group I intron structure. Secondary and tertiary folding of the RNA component of the bI3 RNP are thus not independent: RNA folding is strongly nonhierarchical. These results emphasize that protein-mediated stabilization of RNA tertiary interactions functions to pull the secondary structure into an energetically disfavored, but functional, conformation and emphasize a new role for facilitator proteins in RNP assembly.
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Registered trials
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.