ArticleScientific reports2019
Structural insights into the ability of nucleoplasmin to assemble and chaperone histone octamers for DNA deposition.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 11 citations in OpenAlex.
- Reconstitution of Drosophila and human chromatins by wheat germ cell-free co-expression system.BMC biotechnology · 2020Article
- AtFKBP53: a chimeric histone chaperone with functional nucleoplasmin and PPIase domains.Nucleic acids research · 2020Article
- Structure-function relationship of H2A-H2B specific plant histone chaperones.Cell stress & chaperones · 2020Review
- Histone Chaperone Paralogs Have Redundant, Cooperative, and Divergent Functions in Yeast.Genetics · 2019Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nucleoplasmin (NP) is a pentameric histone chaperone that regulates the condensation state of chromatin in different cellular processes. We focus here on the interaction of NP with the histone octamer, showing that NP could bind sequentially the histone components to assemble an octamer-like particle, and crosslinked octamers with high affinity. The three-dimensional reconstruction of the NP/octamer complex generated by single-particle cryoelectron microscopy, revealed that several intrinsically disordered tail domains of two NP pentamers, facing each other through their distal face, encage the histone octamer in a nucleosome-like conformation and prevent its dissociation. Formation of this complex depended on post-translational modification and exposure of the acidic tract at the tail domain of NP. Finally, NP was capable of transferring the histone octamers to DNA in vitro, assembling nucleosomes. This activity may have biological relevance for processes in which the histone octamer must be rapidly removed from or deposited onto the DNA.
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