ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structural and biochemical analysis of the assembly and function of the yeast pre-mRNA 3' end processing complex CF I.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 24 citations in OpenAlex.
- Surveillance of 3' mRNA cleavage during transcription termination requires CF IB/Hrp1.Nucleic acids research · 2023Article
- Article
- Birth of a poly(A) tail: mechanisms and control of mRNA polyadenylation.FEBS open bio · 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
- System-wide analyses of the fission yeast poly(A)Genome research · 2020Article
- RNA Polymerase II Transcription Attenuation at the Yeast DNA Repair Gene,G3 (Bethesda, Md.) · 2018Article
- Distinct roles of Pcf11 zinc-binding domains in pre-mRNA 3'-end processing.Nucleic acids research · 2017Article
- Applications of NMR to structure determination of RNAs large and small.Archives of biochemistry and biophysics · 2017Review
- 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
- Cleavage factor I links transcription termination to DNA damage response and genome integrity maintenance in Saccharomyces cerevisiae.PLoS genetics · 2014Article
- mRNA fate: Life and death of the mRNA in the cytoplasm.RNA biology · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The accuracy of the 3'-end processing by cleavage and polyadenylation is essential for mRNA biogenesis and transcription termination. In yeast, two poorly conserved neighboring elements upstream of cleavage sites are important for accuracy and efficiency of this process. These two RNA sequences are recognized by the RNA binding proteins Hrp1 and Rna15, but efficient processing in vivo requires a bridging protein (Rna14), which forms a stable dimer of hetero-dimers with Rna15 to stabilize the RNA-protein complex. We earlier reported the structure of the ternary complex of Rna15 and Hrp1 bound to the RNA processing element. We now report the use of solution NMR to study the interaction of Hrp1 with the Rna14-Rna15 heterodimer in the presence and absence of 3'-end processing signals. By using methyl selective labeling on Hrp1, in vivo activity and pull-down assays, we were able to study this complex of several hundred kDa, identify the interface within Hrp1 responsible for recruitment of Rna14 and validate the functional significance of this interaction through structure-driven mutational analysis.
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Registered trials
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