ArticleRNA (New York, N.Y.)2005
The stem-loop binding protein stimulates histone translation at an early step in the initiation pathway.
Article in RNA (New York, N.Y.), 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
What it found
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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
37 citing papers in PubMed, 68 citations in OpenAlex.
- Optimised Ribosome Profiling Reveals New Insights Into Translational Regulation in Synchronised Chlamydomonas reinhardtii Cultures.Plant, cell & environment · 2025Article
- Tailor made: the art of therapeutic mRNA design.Nature reviews. Drug discovery · 2024Review
- 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
- eIF4E and Interactors from Unicellular Eukaryotes.International journal of molecular sciences · 2020Review
- Viral and cellular mRNA-specific activators harness PABP and eIF4G to promote translation initiation downstream of cap binding.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Nickel and cadmium-induced SLBP depletion: A potential pathway to metal mediated cellular transformation.PloS one · 2017Article
- Role of H1 linker histones in mammalian development and stem cell differentiation.Biochimica et biophysica acta · 2016Review
- Modelling Robust Feedback Control Mechanisms That Ensure Reliable Coordination of Histone Gene Expression with DNA Replication.PloS one · 2016Article
- Tethered Function Assays as Tools to Elucidate the Molecular Roles of RNA-Binding Proteins.Advances in experimental medicine and biology · 2016Article
- A multiprotein occupancy map of the mRNP on the 3' end of histone mRNAs.RNA (New York, N.Y.) · 2015Article
- Structure-specific nucleic acid recognition by L-motifs and their diverse roles in expression and regulation of the genome.Biochimica et biophysica acta · 2015Review
- MIF4G domain containing protein regulates cell cycle and hepatic carcinogenesis by antagonizing CDK2-dependent p27 stability.Oncogene · 2015Article
- Thyroid hormone increases bulk histones expression by enhancing translational efficiency.Molecular endocrinology (Baltimore, Md.) · 2015Article
- Profiling post-transcriptionally networked mRNA subsets using RIP-Chip and RIP-Seq.Methods (San Diego, Calif.) · 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
- Structural and biochemical studies of SLIP1-SLBP identify DBP5 and eIF3g as SLIP1-binding proteins.Nucleic acids research · 2013Article
- Assembly of the SLIP1-SLBP complex on histone mRNA requires heterodimerization and sequential binding of SLBP followed by SLIP1.Biochemistry · 2013Article
- Histones: sequestered by Jabba in fatty storehouse.Current biology : CB · 2012Article
- CSR-1 RNAi pathway positively regulates histone expression in C. elegans.The EMBO journal · 2012Article
- INT6 interacts with MIF4GD/SLIP1 and is necessary for efficient histone mRNA translation.RNA (New York, N.Y.) · 2012Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Metazoan replication-dependent histone mRNAs do not have a poly(A) tail but end instead in a conserved stem-loop structure. Efficient translation of these mRNAs is dependent on the stem-loop binding protein (SLBP). Here we explore the mechanism by which SLBP stimulates translation in vertebrate cells, using the tethered function assay and analyzing protein-protein interactions. We show for the first time that translational stimulation by SLBP increases during oocyte maturation and that SLBP stimulates translation at the level of initiation. We demonstrate that SLBP can interact directly with subunit h of eIF3 and with Paip1; however, neither of these interactions is sufficient to mediate its effects on translation. We find that Xenopus SLBP1 functions primarily at an early stage in the cap-dependent initiation pathway, targeting small ribosomal subunit recruitment. Analysis of IRES-driven translation in Xenopus oocytes suggests that SLBP activity requires eIF4E. We propose a model in which a novel factor contacts eIF4E bound to the 5' cap and SLBP bound to the 3' end simultaneously, mediating formation of an alternative end-to-end complex.
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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.