ArticleJournal of molecular biology2010
Novel protein-protein contacts facilitate mRNA 3'-processing signal recognition by Rna15 and Hrp1.
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 29 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
29 citing papers in PubMed, 60 citations in OpenAlex.
- Genetic suppression of precocious transcription termination identifies mutations in essential subunits of the fission yeast cleavage and polyadenylation machinery.RNA (New York, N.Y.) · 2025Article
- Birth of a poly(A) tail: mechanisms and control of mRNA polyadenylation.FEBS open bio · 2023Review
- The Nrd1-Nab3-Sen1 transcription termination complex from a structural perspective.Biochemical Society transactions · 2023Review
- RNA polymerase II transcription attenuation at the yeast DNA repair gene DEF1 is biologically significant and dependent on the Hrp1 RNA-recognition motif.G3 (Bethesda, Md.) · 2023Article
- Structural basis of Nrd1-Nab3 heterodimerization.Life science alliance · 2022Article
- Nucleic acid-protein interfaces studied by MAS solid-state NMR spectroscopy.Journal of structural biology: X · 2022Article
- What Are 3' UTRs Doing?Cold Spring Harbor perspectives in biology · 2019Review
- Activation of the Endonuclease that Defines mRNA 3' Ends Requires Incorporation into an 8-Subunit Core Cleavage and Polyadenylation Factor Complex.Molecular cell · 2019Article
- The structural basis of CstF-77 modulation of cleavage and polyadenylation through stimulation of CstF-64 activity.Nucleic acids research · 2018Article
- Distinct roles of Pcf11 zinc-binding domains in pre-mRNA 3'-end processing.Nucleic acids research · 2017Article
- A structural perspective of RNA recognition by intrinsically disordered proteins.Cellular and molecular life sciences : CMLS · 2016Review
- Dividing and Conquering the Family of RNA Recognition Motifs: A Representative Case Based on hnRNP L.Journal of molecular biology · 2015Article
- Protein-RNA specificity by high-throughput principal component analysis of NMR spectra.Nucleic acids research · 2015Article
- RBFOX and SUP-12 sandwich a G base to cooperatively regulate tissue-specific splicing.Nature structural & molecular biology · 2014Article
- Structural basis of nucleic acid binding by Nicotiana tabacum glycine-rich RNA-binding protein: implications for its RNA chaperone function.Nucleic acids research · 2014Article
- Coordinated and distinct functions of velvet proteins in Fusarium verticillioides.Eukaryotic cell · 2014Article
- Delineating the structural blueprint of the pre-mRNA 3'-end processing machinery.Molecular and cellular biology · 2014Review
- Structure and function of pre-mRNA 5'-end capping quality control and 3'-end processing.Biochemistry · 2014Article
- NMR methods for structural studies of large monomeric and multimeric proteins.Current opinion in structural biology · 2013Review
- Solution structure of the two RNA recognition motifs of hnRNP A1 using segmental isotope labeling: how the relative orientation between RRMs influences the nucleic acid binding topology.Journal of biomolecular NMR · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Precise 3'-end processing of mRNA is essential for correct gene expression, yet in yeast, 3'-processing signals consist of multiple ambiguous sequence elements. Two neighboring elements upstream of the cleavage site are particularly important for the accuracy (positioning element) and efficiency (efficiency element) of 3'-processing and are recognized by the RNA-binding proteins Rna15 and Hrp1, respectively. In vivo, these interactions are strengthened by the scaffolding protein Rna14 that stabilizes their association. The NMR structure of the 34 -kDa ternary complex of the RNA recognition motif (RRM) domains of Hrp1 and Rna15 bound to this pair of RNA elements was determined by residual dipolar coupling and paramagnetic relaxation experiments. It reveals how each of the proteins binds to RNA and introduces a novel class of protein-protein contact in regions of previously unknown function. These interdomain contacts had previously been overlooked in other multi-RRM structures, although a careful analysis suggests that they may be frequently present. Mutations in the regions of these contacts disrupt 3'-end processing, suggesting that they may structurally organize the ribonucleoprotein complexes responsible for RNA processing.
Indexed as
Identifiers
What OpenQuestion holds
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.