ArticleMolecular and cellular biology1999
Stem-loop binding protein facilitates 3'-end formation by stabilizing U7 snRNP binding to histone pre-mRNA.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
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Who cites it
91 citing papers in PubMed, 132 citations in OpenAlex.
- SUMO2 promotes histone pre-mRNA processing by stabilizing histone locus body interactions and facilitating U7 snRNP assembly.Genes & development · 2025Article
- RNA-associated nuclear condensates: Where the nucleus keeps its RNAs in check.Molecules and cells · 2025Review
- Unraveling Histone Loss in Aging and Senescence.Cells · 2024Review
- Improved discovery of RNA-binding protein binding sites in eCLIP data using DEWSeq.Nucleic acids research · 2024Article
- Uridylation of the histone mRNA stem-loop weakens binding interactions with SLBP while maintaining interactions with 3'hExo.RNA biology · 2023Article
- Human cytomegalovirus lytic infection inhibits replication-dependent histone synthesis and requires stem loop binding protein function.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- U7 deciphered: the mechanism that forms the unusual 3' end of metazoan replication-dependent histone mRNAs.Biochemical Society transactions · 2021Review
- 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
- 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
- ALYREF links 3'-end processing to nuclear export of non-polyadenylated mRNAs.The EMBO journal · 2019Article
- Histone supply: Multitiered regulation ensures chromatin dynamics throughout the cell cycle.The Journal of cell biology · 2019Review
- Article
- 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
- Transcription elongation rate affects nascent histone pre-mRNA folding and 3' end processing.Genes & development · 2018Article
- Ovarian transcriptomic analysis of Shan Ma ducks at peak and late stages of egg production.Asian-Australasian journal of animal sciences · 2017Article
- U7 snRNP is recruited to histone pre-mRNA in a FLASH-dependent manner by two separate regions of the stem-loop binding protein.RNA (New York, N.Y.) · 2017Article
- Guard the guardian: A CRL4 ligase stands watch over histone production.Nucleus (Austin, Tex.) · 2017Review
- Nickel and cadmium-induced SLBP depletion: A potential pathway to metal mediated cellular transformation.PloS one · 2017Article
31 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The 3' end of histone mRNA is formed by an endonucleolytic cleavage of the primary transcript after a conserved stem-loop sequence. The cleavage reaction requires at least two trans-acting factors: the stem-loop binding protein (SLBP), which binds the stem-loop sequence, and the U7 snRNP that interacts with a sequence downstream from the cleavage site. Removal of SLBP from a nuclear extract abolishes 3'-end processing, and the addition of recombinant SLBP restores processing activity of the depleted extract. To determine the regions of human SLBP necessary for 3' processing, various deletion mutants of the protein were tested for their ability to complement the SLBP-depleted extract. The entire N-terminal domain and the majority of the C-terminal domain of human SLBP are dispensable for processing. The minimal protein that efficiently supports cleavage of histone pre-mRNA consists of 93 amino acids containing the 73-amino-acid RNA-binding domain and 20 amino acids located immediately next to its C terminus. Replacement of these 20 residues with an unrelated sequence in the context of the full-length SLBP reduces processing >90%. Coimmunoprecipitation experiments with the anti-SLBP antibody demonstrated that SLBP and U7 snRNP form a stable complex only in the presence of pre-mRNA substrates containing a properly positioned U7 snRNP binding site. One role of SLBP is to stabilize the interaction of the histone pre-mRNA with U7 snRNP.
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