ArticleMolecular and cellular biology2009
Studies of the 5' exonuclease and endonuclease activities of CPSF-73 in histone pre-mRNA processing.
Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 66 citations in OpenAlex.
- Multiple Forms and Functions of Premature Termination by RNA Polymerase II.Journal of molecular biology · 2025Review
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- Modulation of diverse biological processes by CPSF, the master regulator of mRNA 3' ends.RNA (New York, N.Y.) · 2024Review
- Article
- Xrn2 substrate mapping identifies torpedo loading sites and extensive premature termination of RNA pol II transcription.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
- Reconstitution and biochemical assays of an active human histone pre-mRNA 3'-end processing machinery.Methods in enzymology · 2021Article
- The Integrator Complex in Transcription and Development.Trends in biochemical sciences · 2020Review
- Studies with recombinant U7 snRNP demonstrate that CPSF73 is both an endonuclease and a 5'-3' exonuclease.RNA (New York, N.Y.) · 2020Article
- The conserved ribonuclease aCPSF1 triggers genome-wide transcription termination of Archaea via a 3'-end cleavage mode.Nucleic acids research · 2020Article
- Plant Ribonuclease J: An Essential Player in Maintaining Chloroplast RNA Quality Control for Gene Expression.Plants (Basel, Switzerland) · 2020Review
- Composition and processing activity of a semi-recombinant holo U7 snRNP.Nucleic acids research · 2020Article
- Structure of an active human histone pre-mRNA 3'-end processing machinery.Science (New York, N.Y.) · 2020Article
- The torpedo effect in Bacillus subtilis: RNase J1 resolves stalled transcription complexes.The EMBO journal · 2020Article
- TheGenome research · 2019Article
- The Integrator complex cleaves nascent mRNAs to attenuate transcription.Genes & development · 2019Article
- Barcoding chemical modifications into nucleic acids improves drug stabilityJournal of materials chemistry. B · 2018Article
- Protein composition of catalytically active U7-dependent processing complexes assembled on histone pre-mRNA containing biotin and a photo-cleavable linker.Nucleic acids research · 2018Article
- Functional Analysis of RNA Interference-Related Soybean Pod Borer (Frontiers in physiology · 2018Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Processing of histone pre-mRNA requires a single 3' endonucleolytic cleavage guided by the U7 snRNP that binds downstream of the cleavage site. Following cleavage, the downstream cleavage product (DCP) is rapidly degraded in vitro by a nuclease that also depends on the U7 snRNP. Our previous studies demonstrated that the endonucleolytic cleavage is catalyzed by the cleavage/polyadenylation factor CPSF-73. Here, by using RNA substrates with different nucleotide modifications, we characterize the activity that degrades the DCP. We show that the degradation is blocked by a 2'-O-methyl nucleotide and occurs in the 5'-to-3' direction. The U7-dependent 5' exonuclease activity is processive and continues degrading the DCP substrate even after complete removal of the U7-binding site. Thus, U7 snRNP is required only to initiate the degradation. UV cross-linking studies demonstrate that the DCP and its 5'-truncated version specifically interact with CPSF-73, strongly suggesting that in vitro, the same protein is responsible for the endonucleolytic cleavage of histone pre-mRNA and the subsequent degradation of the DCP. By using various RNA substrates, we define important space requirements upstream and downstream of the cleavage site that dictate whether CPSF-73 functions as an endonuclease or a 5' exonuclease. RNA interference experiments with HeLa cells indicate that degradation of the DCP does not depend on the Xrn2 5' exonuclease, suggesting that CPSF-73 degrades the DCP both in vitro and in vivo.
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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.