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Drosophila histone locus bodies form by hierarchical recruitment of components.
J Cell Biol. 2011 May 16; 193(4):677-94
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08 Jun 2011
New Finding
DOI: 10.3410/f.11076956.12030054
This study reveals new mechanistic insights on the formation of a nuclear body.
The authors showed that the histone locus body (HLB), observed as nuclear foci enriched with U7 small nuclear RNA (snRNA) and containing the cell cycle-regulated histone gene clusters, is assembled in a stepwise process.
HLBs...Continue reading
The authors showed that the histone locus body (HLB), observed as nuclear foci enriched with U7 small nuclear RNA (snRNA) and containing the cell cycle-regulated histone gene clusters, is assembled in a stepwise process.
HLBs...Continue reading
This study reveals new mechanistic insights on the formation of a nuclear body.
The authors showed that the histone locus body (HLB), observed as nuclear foci enriched with U7 small nuclear RNA (snRNA) and containing the cell cycle-regulated histone gene clusters, is assembled in a stepwise process.
HLBs are critical for proper histone gene expression and pre-mRNA processing. The authors took a two-pronged approach (proteomics and an RNAi screen) to identify HLB components. Among them, multisex combs (Mxc), a potential homologue to the mammalian HLB protein NPAT, is necessary for proper activation of the histone H3 promoter and histone pre-mRNA processing. Surprisingly, transcription of the histone gene clusters was not required for recruitment of some HLB components, a subset of which remains assembled throughout the cell cycle. Together, these data demonstrate the dynamic complexities of HLB formation, which may extend to other types of nuclear bodies.
The authors showed that the histone locus body (HLB), observed as nuclear foci enriched with U7 small nuclear RNA (snRNA) and containing the cell cycle-regulated histone gene clusters, is assembled in a stepwise process.
HLBs are critical for proper histone gene expression and pre-mRNA processing. The authors took a two-pronged approach (proteomics and an RNAi screen) to identify HLB components. Among them, multisex combs (Mxc), a potential homologue to the mammalian HLB protein NPAT, is necessary for proper activation of the histone H3 promoter and histone pre-mRNA processing. Surprisingly, transcription of the histone gene clusters was not required for recruitment of some HLB components, a subset of which remains assembled throughout the cell cycle. Together, these data demonstrate the dynamic complexities of HLB formation, which may extend to other types of nuclear bodies.
Disclosures
None declared
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Wallrath L and Vitalini M: F1000Prime Recommendation of [White AE et al., J Cell Biol 2011, 193(4):677-94]. In F1000Prime, 08 Jun 2011; DOI: 10.3410/f.11076956.12030054. F1000Prime.com/11076956#eval12030054
F1000Prime Recommendations, Dissents and Comments for [White AE et al., J Cell Biol 2011, 193(4):677-94]. In F1000Prime, 26 May 2013; F1000Prime.com/11076956
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Nuclear bodies are protein- and RNA-containing structures that participate in a wide range of processes critical to genome function. Molecular self-organization is thought to drive nuclear body formation, but whether this occurs stochastically or via an ordered, hierarchical process is not fully understood. We addressed this question using RNAi and proteomic approaches in Drosophila melanogaster to identify and characterize novel components of the histone locus body (HLB), a nuclear body involved in the expression of replication-dependent histone genes. We identified the transcription elongation factor suppressor of Ty 6 (Spt6) and a homologue of mammalian nuclear protein of the ataxia telangiectasia-mutated locus that is encoded by the homeotic gene multisex combs (mxc) as novel HLB components. By combining genetic manipulation in both cell culture and embryos with cytological observations of Mxc, Spt6, and the known HLB components, FLICE-associated huge protein, Mute, U7 small nuclear ribonucleoprotein, and MPM-2 phosphoepitope, we demonstrated sequential recruitment and hierarchical dependency for localization of factors to HLBs during development, suggesting that ordered assembly can play a role in nuclear body formation.
PMID: 21576393
