Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release

Christopher Warren, Tsutomu Matsui, Jerome M. Karp, Takashi Onikubo, Sean Cahill, Michael Brenowitz, David Cowburn, Mark Girvin and David Shechter ()
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Christopher Warren: Albert Einstein College of Medicine
Tsutomu Matsui: Stanford Synchrotron Radiation Lightsource
Jerome M. Karp: Albert Einstein College of Medicine
Takashi Onikubo: Albert Einstein College of Medicine
Sean Cahill: Albert Einstein College of Medicine
Michael Brenowitz: Albert Einstein College of Medicine
David Cowburn: Albert Einstein College of Medicine
Mark Girvin: Albert Einstein College of Medicine
David Shechter: Albert Einstein College of Medicine

Nature Communications, 2017, vol. 8, issue 1, 1-16

Abstract: Abstract Nucleoplasmin (Npm) is a highly conserved histone chaperone responsible for the maternal storage and zygotic release of histones H2A/H2B. Npm contains a pentameric N-terminal core domain and an intrinsically disordered C-terminal tail domain. Though intrinsically disordered regions are common among histone chaperones, their roles in histone binding and chaperoning remain unclear. Using an NMR-based approach, here we demonstrate that the Xenopus laevis Npm tail domain controls the binding of histones at its largest acidic stretch (A2) via direct competition with both the C-terminal basic stretch and basic nuclear localization signal. NMR and small-angle X-ray scattering (SAXS) structural analyses allowed us to construct models of both the tail domain and the pentameric complex. Functional analyses demonstrate that these competitive intramolecular interactions negatively regulate Npm histone chaperone activity in vitro. Together these data establish a potentially generalizable mechanism of histone chaperone regulation via dynamic and specific intramolecular shielding of histone interaction sites.

Date: 2017
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DOI: 10.1038/s41467-017-02308-3

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