ArticleMolecular biology of the cell2015
Distinct self-interaction domains promote Multi Sex Combs accumulation in and formation of the Drosophila histone locus body.
Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 59 citations in OpenAlex.
- Cycling off: a novel mechanism for differential cell cycle-dependent histone gene expression.Genes & development · 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
- The functional organization of chromosome territories in single nuclei during zygotic genome activation.Scientific reports · 2026Article
- Cell-cycle-dependent repression of histone gene transcription by histone H4.Nature structural & molecular biology · 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
- Cell-cycle-regulated transcriptional pausing ofMolecular biology of the cell · 2025Article
- The functional organization of chromosome territories in single nuclei during zygotic genome activation.bioRxiv : the preprint server for biology · 2025Article
- Zelda is dispensable forMolecular biology of the cell · 2025Article
- Directed stochasticity: Building biomolecular condensates in the right place.The Journal of cell biology · 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
- Article
- Germline NPAT inactivating variants as cause of hereditary colorectal cancer.European journal of human genetics : EJHG · 2024Article
- Article
- Sequence reliance of abioRxiv : the preprint server for biology · 2023Article
- Histone locus bodies: a paradigm for how nuclear biomolecular condensates control cell cycle regulated gene expression.Nucleus (Austin, Tex.) · 2023Review
- Coordinated expression of replication-dependent histone genes from multiple loci promotes histone homeostasis inMolecular biology of the cell · 2023Article
Corrections and comments
- Erratum issuedCorrection.2015
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Nuclear bodies (NBs) are structures that concentrate proteins, RNAs, and ribonucleoproteins that perform functions essential to gene expression. How NBs assemble is not well understood. We studied the Drosophila histone locus body (HLB), a NB that concentrates factors required for histone mRNA biosynthesis at the replication-dependent histone gene locus. We coupled biochemical analysis with confocal imaging of both fixed and live tissues to demonstrate that the Drosophila Multi Sex Combs (Mxc) protein contains multiple domains necessary for HLB assembly. An important feature of this assembly process is the self-interaction of Mxc via two conserved N-terminal domains: a LisH domain and a novel self-interaction facilitator (SIF) domain immediately downstream of the LisH domain. Molecular modeling suggests that the LisH and SIF domains directly interact, and mutation of either the LisH or the SIF domain severely impairs Mxc function in vivo, resulting in reduced histone mRNA accumulation. A region of Mxc between amino acids 721 and 1481 is also necessary for HLB assembly independent of the LisH and SIF domains. Finally, the C-terminal 195 amino acids of Mxc are required for recruiting FLASH, an essential histone mRNA-processing factor, to the HLB. We conclude that multiple domains of the Mxc protein promote HLB assembly in order to concentrate factors required for histone mRNA biosynthesis.
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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.