Structural Insights into the Ability of Nucleoplasmin to Assemble and Chaperone Histone Octamers for DNA Deposition

Overview

Journal Sci Rep

Specialty Science

Date 2019 Jul 3

PMID 31263230

Citations 4

Authors

Aitor Franco

Rocio Arranz

Noelia Fernandez-Rivero

Adrian Velazquez-Campoy

Jaime Martin-Benito

Joan Segura

Adelina Prado

Jose M Valpuesta

Arturo Muga

Affiliations

Soon will be listed here.

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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