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Developmentally Regulated Post-translational Modification of Nucleoplasmin Controls Histone Sequestration and Deposition.

Abstract：

:Nucleoplasmin (Npm) is an abundant histone chaperone in vertebrate oocytes and embryos. During embryogenesis, regulation of Npm histone binding is critical for its function in storing and releasing maternal histones to establish and maintain the zygotic epigenome. Here, we demonstrate that Xenopus laevis Npm post-translational modifications (PTMs) specific to the oocyte and egg promote either histone deposition or sequestration, respectively. Mass spectrometry and Npm phosphomimetic mutations used in chromatin assembly assays identified hyperphosphorylation on the N-terminal tail as a critical regulator for sequestration. C-terminal tail phosphorylation and PRMT5-catalyzed arginine methylation enhance nucleosome assembly by promoting histone interaction with the second acidic tract of Npm. Electron microscopy reconstructions of Npm and TTLL4 activity toward the C-terminal tail demonstrate that oocyte- and egg-specific PTMs cause Npm conformational changes. Our results reveal that PTMs regulate Npm chaperoning activity by modulating Npm conformation and Npm-histone interaction, leading to histone sequestration in the egg.

journal_name

Cell Rep

journal_title

Cell reports

authors

Onikubo T,Nicklay JJ,Xing L,Warren C,Anson B,Wang WL,Burgos ES,Ruff SE,Shabanowitz J,Cheng RH,Hunt DF,Shechter D

doi

10.1016/j.celrep.2015.02.038

subject

Has Abstract

pub_date

2015-03-17 00:00:00

pages

1735-1748

issue

10

issn

2211-1247

pii

S2211-1247(15)00196-5

journal_volume

10

pub_type

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