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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Warren C,Matsui T,Karp JM,Onikubo T,Cahill S,Brenowitz M,Cowburn D,Girvin M,Shechter Ddoi
10.1038/s41467-017-02308-3subject
Has Abstractpub_date
2017-12-20 00:00:00pages
2215issue
1issn
2041-1723pii
10.1038/s41467-017-02308-3journal_volume
8pub_type
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