ArticleNucleic acids research2004
Rna14-Rna15 assembly mediates the RNA-binding capability of Saccharomyces cerevisiae cleavage factor IA.
Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 41 citations in OpenAlex.
- Surveillance of 3' mRNA cleavage during transcription termination requires CF IB/Hrp1.Nucleic acids research · 2023Article
- Fission yeast Ctf1, a cleavage and polyadenylation factor subunit is required for the maintenance of genomic integrity.Molecular genetics and genomics : MGG · 2017Article
- Distinct roles of Pcf11 zinc-binding domains in pre-mRNA 3'-end processing.Nucleic acids research · 2017Article
- Co-transcriptional mRNP formation is coordinated within a molecular mRNP packaging station in S. cerevisiae.BioEssays : news and reviews in molecular, cellular and developmental biology · 2015Review
- RPRD1A and RPRD1B are human RNA polymerase II C-terminal domain scaffolds for Ser5 dephosphorylation.Nature structural & molecular biology · 2014Article
- Delineating the structural blueprint of the pre-mRNA 3'-end processing machinery.Molecular and cellular biology · 2014Review
- Structural and biochemical analysis of the assembly and function of the yeast pre-mRNA 3' end processing complex CF I.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Crystal structure of the Rna14-Rna15 complex.RNA (New York, N.Y.) · 2012Article
- The interaction of Pcf11 and Clp1 is needed for mRNA 3'-end formation and is modulated by amino acids in the ATP-binding site.Nucleic acids research · 2012Article
- Reconstitution of CF IA from overexpressed subunits reveals stoichiometry and provides insights into molecular topology.Biochemistry · 2011Article
- Hexameric architecture of CstF supported by CstF-50 homodimerization domain structure.RNA (New York, N.Y.) · 2011Article
- Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain.Nature structural & molecular biology · 2010Article
- Novel protein-protein contacts facilitate mRNA 3'-processing signal recognition by Rna15 and Hrp1.Journal of molecular biology · 2010Article
- Structure of the Rna15 RRM-RNA complex reveals the molecular basis of GU specificity in transcriptional 3'-end processing factors.Nucleic acids research · 2010Article
- Hydrodynamic characterization of the SufBC and SufCD complexes and their interaction with fluorescent adenosine nucleotides.Protein science : a publication of the Protein Society · 2008Article
- Polyadenylation site choice in yeast is affected by competition between Npl3 and polyadenylation factor CFI.RNA (New York, N.Y.) · 2007Article
- MLN51 stimulates the RNA-helicase activity of eIF4AIII.PloS one · 2007Article
- The structure of the CstF-77 homodimer provides insights into CstF assembly.Nucleic acids research · 2007Article
- Structure of a nucleotide-bound Clp1-Pcf11 polyadenylation factor.Nucleic acids research · 2007Article
- RNA polymerase II CTD phosphopeptides compete with RNA for the interaction with Pcf11.RNA (New York, N.Y.) · 2006Article
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
The Rna14-Rna15 complex is a core component of the cleavage factor IA RNA-processing complex from Saccharomyces cerevisiae. To understand the assembly and RNA-binding properties, we have isolated and characterized the Rna14-Rna15 complex using a combination of biochemical and biophysical methods. Analysis of the purified complex, using transmission electron microscopy, reveals that the two proteins assemble into a kinked rod-shaped structure and that these rods are able to further self-associate. Analytical ultracentrifugation reveals that Rna14 mediates this association and facilitates assembly of an A2B2 tetramer (M(r) 230 000), where relatively compact Rna14-Rna15 heterodimers are in rapid equilibrium with tetramers that have a more extended shape. The Rna14-Rna15 complex, unlike the individual components, binds to an RNA oligonucleotide derived from the 3'-untranslated region of the S.cerevisiae GAL7 gene. Based on these structural and thermodynamic data, we propose that CFIA assembly regulates RNA-binding activity.
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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.