ArticleNucleic acids research2004
SLBP is associated with histone mRNA on polyribosomes as a component of the histone mRNP.
Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 59 citations in OpenAlex.
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- Mechanistic insights into recruitment and regulation of the RNA helicase UPF1 in replication-dependent histone mRNA decay.Nature communications · 2026Article
- Histone supply: a precious commodity for cell identity.The Biochemical journal · 2025Review
- Mudskipper detects combinatorial RNA binding protein interactions in multiplexed CLIP data.Cell genomics · 2024Article
- The Role of Dendritic Cells in the Host Response to Marek's Disease Virus (MDV) as Shown by Transcriptomic Analysis of Susceptible and Resistant Birds.Pathogens (Basel, Switzerland) · 2022Article
- 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
- Distinct features of the Leishmania cap-binding protein LeishIF4E2 revealed by CRISPR-Cas9 mediated hemizygous deletion.PLoS neglected tropical diseases · 2021Article
- A region of SLBP outside the mRNA-processing domain is essential for deposition of histone mRNA into theJournal of cell science · 2021Article
- A heterogeneous cellular response to ionizing radiation revealed by single cell transcriptome sequencing.American journal of cancer research · 2021Article
- Role of oligouridylation in normal metabolism and regulated degradation of mammalian histone mRNAs.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Article
- Mapping the Interaction Network of Key Proteins Involved in Histone mRNA Generation: A Hydrogen/Deuterium Exchange Study.Journal of molecular biology · 2016Article
- Modelling Robust Feedback Control Mechanisms That Ensure Reliable Coordination of Histone Gene Expression with DNA Replication.PloS one · 2016Article
- A multiprotein occupancy map of the mRNP on the 3' end of histone mRNAs.RNA (New York, N.Y.) · 2015Article
- A Potential New Mechanism of Arsenic Carcinogenesis: Depletion of Stem-Loop Binding Protein and Increase in Polyadenylated Canonical Histone H3.1 mRNA.Biological trace element research · 2015Article
- Thyroid hormone increases bulk histones expression by enhancing translational efficiency.Molecular endocrinology (Baltimore, Md.) · 2015Article
- Arsenic induces polyadenylation of canonical histone mRNA by down-regulating stem-loop-binding protein gene expression.The Journal of biological chemistry · 2014Article
- Replication stress-induced alternative mRNA splicing alters properties of the histone RNA-binding protein HBP/SLBP: a key factor in the control of histone gene expression.Bioscience reports · 2013Article
- Deciphering the modulation of gene expression by type I and II interferons combining 4sU-tagging, translational arrest and in silico promoter analysis.Nucleic acids research · 2013Article
- RNA-protein analysis using a conditional CRISPR nuclease.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The stem-loop binding protein (SLBP) binds the 3' end of histone mRNA and is present both in nucleus, and in the cytoplasm on the polyribosomes. SLBP participates in the processing of the histone pre-mRNA and in translation of the mature message. Histone mRNAs are rapidly degraded when cells are treated with inhibitors of DNA replication and are stabilized by inhibitors of translation, resulting in an increase in histone mRNA levels. Here, we show that SLBP is a component of the histone messenger ribonucleoprotein particle (mRNP). Histone mRNA from polyribosomes is immunoprecipitated with anti-SLBP. Most of the SLBP in cycloheximide-treated cells is present on polyribosomes as a result of continued synthesis and transport of the histone mRNP to the cytoplasm. When cells are treated with inhibitors of DNA replication, histone mRNAs are rapidly degraded but SLBP levels remain constant and SLBP is relocalized to the nucleus. SLBP remains active both in RNA binding and histone pre-mRNA processing when DNA replication is inhibited.
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