ArticleThe Journal of biological chemistry2014
A conserved interaction that is essential for the biogenesis of histone locus bodies.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 54 citations in OpenAlex.
- Are components of the histone gene expression machinery functionally repurposed in terminally differentiated cells?Biology open · 2026Article
- Differential control of both cell cycle-regulated and quantitative histone mRNA expression bybioRxiv : the preprint server for biology · 2026Article
- Human CRAMP1 specifically promotes the expression of histone H1 genes.EMBO reports · 2026Article
- ENY2 Protein Is Present at the Histone Locus Body HLB As Part of Complexes with Different Functions in Transcription and mRNA Export.Doklady. Biochemistry and biophysics · 2026Article
- SAGA Transcription Coactivator Complex Is Associated with Histone Locus Body HLB.Doklady. Biochemistry and biophysics · 2025Article
- TREX-2 mRNA Export Complex Interacts with HLB Component FLASH and Is Recruited to Processed Histone mRNAs.Doklady. Biochemistry and biophysics · 2025Article
- CRAMP1-dependent histone H1 biogenesis is essential for topoisomerase II inhibitor tolerance.Molecular cell · 2025Article
- Cell-cycle-regulated transcriptional pausing ofMolecular biology of the cell · 2025Article
- KPNA3 regulates histone locus body formation by modulating condensation and nuclear import of NPAT.The Journal of cell biology · 2025Article
- Cell cycle-regulated transcriptional pausing ofbioRxiv : the preprint server for biology · 2024Article
- Cut&tag: a powerful epigenetic tool for chromatin profiling.Epigenetics · 2024Review
- Multiple roles of arsenic compounds in phase separation and membraneless organelles formation determine their therapeutic efficacy in tumors.Journal of pharmaceutical analysis · 2024Review
- Dual role of CASP8AP2/FLASH in regulating epithelial-to-mesenchymal transition plasticity (EMP).Translational oncology · 2024Article
- Histone locus bodies: a paradigm for how nuclear biomolecular condensates control cell cycle regulated gene expression.Nucleus (Austin, Tex.) · 2023Review
- A bioinformatics screen reveals hox and chromatin remodeling factors at the Drosophila histone locus.BMC genomic data · 2023Article
- Article
- A bioinformatics screen reveals Hox and chromatin remodeling factors at thebioRxiv : the preprint server for biology · 2023Article
- Human histone pre-mRNA assembles histone or canonical mRNA-processing complexes by overlapping 3'-end sequence elements.Nucleic acids research · 2022Article
- Mxc, a Drosophila homolog of mental retardation-associated gene NPAT, maintains neural stem cell fate.Cell & bioscience · 2022Article
- Epigenetic-Mediated Regulation of Gene Expression for Biological Control and Cancer: Cell and Tissue Structure, Function, and Phenotype.Results and problems in cell differentiation · 2022Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Nuclear protein, ataxia-telangiectasia locus (NPAT) and FLICE-associated huge protein (FLASH) are two major components of discrete nuclear structures called histone locus bodies (HLBs). NPAT is a key co-activator of histone gene transcription, whereas FLASH through its N-terminal region functions in 3' end processing of histone primary transcripts. The C-terminal region of FLASH contains a highly conserved domain that is also present at the end of Yin Yang 1-associated protein-related protein (YARP) and its Drosophila homologue, Mute, previously shown to localize to HLBs in Drosophila cells. Here, we show that the C-terminal domain of human FLASH and YARP interacts with the C-terminal region of NPAT and that this interaction is essential and sufficient to drive FLASH and YARP to HLBs in HeLa cells. Strikingly, only the last 16 amino acids of NPAT are sufficient for the interaction. We also show that the C-terminal domain of Mute interacts with a short region at the end of the Drosophila NPAT orthologue, multi sex combs (Mxc). Altogether, our data indicate that the conserved C-terminal domain shared by FLASH, YARP, and Mute recognizes the C-terminal sequence of NPAT orthologues, thus acting as a signal targeting proteins to HLBs. Finally, we demonstrate that the C-terminal domain of human FLASH can be directly joined with its N-terminal region through alternative splicing. The resulting 190-amino acid MiniFLASH, despite lacking 90% of full-length FLASH, contains all regions necessary for 3' end processing of histone pre-mRNA in vitro and accumulates in HLBs.
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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.