ArticleRNA (New York, N.Y.)2020
Studies with recombinant U7 snRNP demonstrate that CPSF73 is both an endonuclease and a 5'-3' exonuclease.
Article in RNA (New York, N.Y.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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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.
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Who cites it
20 citing papers in PubMed, 26 citations in OpenAlex.
- An N-terminal helix of Lsm11 stabilizes CPSF73 in U7 snRNP for histone pre-mRNA 3'-end processing.Nucleic acids research · 2026Article
- Proteins that recognize unique features of U7 snRNA and may substitute for Gemin5 in the assembly of U7-specific Sm ring.RNA (New York, N.Y.) · 2025Article
- DNA-directed termination of mammalian RNA polymerase II.Genes & development · 2024Article
- Modulation of diverse biological processes by CPSF, the master regulator of mRNA 3' ends.RNA (New York, N.Y.) · 2024Review
- CPSF3 inhibition blocks pancreatic cancer cell proliferation through disruption of core histone mRNA processing.RNA (New York, N.Y.) · 2024Article
- Histone locus bodies: a paradigm for how nuclear biomolecular condensates control cell cycle regulated gene expression.Nucleus (Austin, Tex.) · 2023Review
- In vitro methylation of the U7 snRNP subunits Lsm11 and SmE by the PRMT5/MEP50/pICln methylosome.RNA (New York, N.Y.) · 2023Article
- Article
- Knowing when to stop: Transcription termination on protein-coding genes by eukaryotic RNAPII.Molecular cell · 2023Review
- Human histone pre-mRNA assembles histone or canonical mRNA-processing complexes by overlapping 3'-end sequence elements.Nucleic acids research · 2022Article
- Xrn2 substrate mapping identifies torpedo loading sites and extensive premature termination of RNA pol II transcription.Genes & development · 2022Article
- Molecular Insights into mRNA Polyadenylation and Deadenylation.International journal of molecular sciences · 2022Review
- Reconstitution of 3' end processing of mammalian pre-mRNA reveals a central role of RBBP6.Genes & development · 2022Article
- U7 deciphered: the mechanism that forms the unusual 3' end of metazoan replication-dependent histone mRNAs.Biochemical Society transactions · 2021Review
- β-CASP proteins removing RNA polymerase from DNA: when a torpedo is needed to shoot a sitting duck.Nucleic acids research · 2021Review
- A real-time fluorescence assay for CPSF73, the nuclease for pre-mRNA 3'-end processing.RNA (New York, N.Y.) · 2021Article
- On the Cutting Edge: Regulation and Therapeutic Potential of the mRNA 3' End Nuclease.Trends in biochemical sciences · 2021Review
- Comparative parallel analysis of RNA ends identifies mRNA substrates of a tRNA splicing endonuclease-initiated mRNA decay pathway.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Reconstitution and biochemical assays of an active human histone pre-mRNA 3'-end processing machinery.Methods in enzymology · 2021Article
- 3' Processing of Animal Replication-Dependent Histone mRNAs.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Metazoan replication-dependent histone pre-mRNAs are cleaved at the 3' end by U7 snRNP, an RNA-guided endonuclease that contains U7 snRNA, seven proteins of the Sm ring, FLASH, and four polyadenylation factors: symplekin, CPSF73, CPSF100, and CstF64. A fully recombinant U7 snRNP was recently reconstituted from all 13 components for functional and structural studies and shown to accurately cleave histone pre-mRNAs. Here, we analyzed the activity of recombinant U7 snRNP in more detail. We demonstrate that in addition to cleaving histone pre-mRNAs endonucleolytically, reconstituted U7 snRNP acts as a 5'-3' exonuclease that degrades the downstream product generated from histone pre-mRNAs as a result of the endonucleolytic cleavage. Surprisingly, recombinant U7 snRNP also acts as an endonuclease on single-stranded DNA substrates. All these activities depend on the ability of U7 snRNA to base-pair with the substrate and on the presence of the amino-terminal domain (NTD) of symplekin in either
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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.