ArticleNucleic acids research2018
Protein composition of catalytically active U7-dependent processing complexes assembled on histone pre-mRNA containing biotin and a photo-cleavable linker.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 29 citations in OpenAlex.
- Are components of the histone gene expression machinery functionally repurposed in terminally differentiated cells?Biology open · 2026Article
- 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
- Cell-cycle-regulated transcriptional pausing ofMolecular biology of the cell · 2025Article
- The CFII components PCF11 and Cbc change subnuclear localization as cells differentiate in an adult stem cell lineage.microPublication biology · 2025Article
- Cell cycle-regulated transcriptional pausing ofbioRxiv : the preprint server for biology · 2024Article
- A developmental mechanism to regulate alternative polyadenylation in an adult stem cell lineage.Genes & development · 2024Article
- A Developmental Mechanism to Regulate Alternative Polyadenylation in an Adult Stem Cell Lineage.bioRxiv : the preprint server for biology · 2024Article
- Anticancer benzoxaboroles block pre-mRNA processing by directly inhibiting CPSF3.Cell chemical biology · 2024Article
- In vitro methylation of the U7 snRNP subunits Lsm11 and SmE by the PRMT5/MEP50/pICln methylosome.RNA (New York, N.Y.) · 2023Article
- 3'-End Processing of Eukaryotic mRNA: Machinery, Regulation, and Impact on Gene Expression.Annual review of biochemistry · 2023Review
- Human histone pre-mRNA assembles histone or canonical mRNA-processing complexes by overlapping 3'-end sequence elements.Nucleic acids research · 2022Article
- The 3' Pol II pausing at replication-dependent histone genes is regulated by Mediator through Cajal bodies' association with histone locus bodies.Nature communications · 2022Article
- RBBP6 activates the pre-mRNA 3' end processing machinery in humans.Genes & development · 2022Article
- U7 deciphered: the mechanism that forms the unusual 3' end of metazoan replication-dependent histone mRNAs.Biochemical Society transactions · 2021Review
- On the Cutting Edge: Regulation and Therapeutic Potential of the mRNA 3' End Nuclease.Trends in biochemical sciences · 2021Review
- Superresolution light microscopy of theMolecular biology of the cell · 2021Article
- Reconstitution and biochemical assays of an active human histone pre-mRNA 3'-end processing machinery.Methods in enzymology · 2021Article
- Studies with recombinant U7 snRNP demonstrate that CPSF73 is both an endonuclease and a 5'-3' exonuclease.RNA (New York, N.Y.) · 2020Article
- The role of Mediator and Little Elongation Complex in transcription termination.Nature communications · 2020Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
3' end cleavage of metazoan replication-dependent histone pre-mRNAs requires the multi-subunit holo-U7 snRNP and the stem-loop binding protein (SLBP). The exact composition of the U7 snRNP and details of SLBP function in processing remain unclear. To identify components of the U7 snRNP in an unbiased manner, we developed a novel approach for purifying processing complexes from Drosophila and mouse nuclear extracts. In this method, catalytically active processing complexes are assembled in vitro on a cleavage-resistant histone pre-mRNA containing biotin and a photo-sensitive linker, and eluted from streptavidin beads by UV irradiation for direct analysis by mass spectrometry. In the purified processing complexes, Drosophila and mouse U7 snRNP have a remarkably similar composition, always being associated with CPSF73, CPSF100, symplekin and CstF64. Many other proteins previously implicated in the U7-dependent processing are not present. Drosophila U7 snRNP bound to histone pre-mRNA in the absence of SLBP contains the same subset of polyadenylation factors but is catalytically inactive and addition of recombinant SLBP is sufficient to trigger cleavage. This result suggests that Drosophila SLBP promotes a structural rearrangement of the processing complex, resulting in juxtaposition of the CPSF73 endonuclease with the cleavage site in the pre-mRNA substrate.
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