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TitleStructural insights into the ability of nucleoplasmin to assemble and chaperone histone octamers for DNA deposition.
Journal, issue, pagesSci Rep, Vol. 9, Issue 1, Page 9487, Year 2019
Publish dateJul 1, 2019
AuthorsAitor Franco / Rocío Arranz / Noelia Fernández-Rivero / Adrián Velázquez-Campoy / Jaime Martín-Benito / Joan Segura / Adelina Prado / José M Valpuesta / Arturo Muga /
PubMed AbstractNucleoplasmin (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 ...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.
External linksSci Rep / PubMed:31263230 / PubMed Central
MethodsEM (single particle)
Resolution14.7 Å
Structure data

EMDB-0323:
Structural insights into the ability of nucleoplasmin to assemble and chaperone histone octamers for DNA deposition
Method: EM (single particle) / Resolution: 14.7 Å

Source
  • Xenopus laevis (African clawed frog)
  • Gallus gallus (chicken)

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