ArticleNature communications2017
Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 28 citations in OpenAlex.
- Multisite phosphorylation of the AML-linked C-terminal of nucleophosmin (NPM1) orchestrates protein stability, DNA binding and charge block-driven phase separation.Nucleic acids research · 2026Article
- Peptide Inhibitors Targeting FOXO4-p53 Interactions and Inducing Senescent Cancer Cell-specific Apoptosis.Journal of medicinal chemistry · 2025Article
- Glutamylation of Npm2 and Nap1 acidic disordered regions increases DNA mimicry and histone chaperone efficiency.iScience · 2024Article
- Plant-specific HDT family histone deacetylases are nucleoplasmins.The Plant cell · 2022Article
- Allostery governs Cdk2 activation and differential recognition of CDK inhibitors.Nature chemical biology · 2021Article
- Peptide Assemblies Mimicking Chaperones for Protein Trafficking.Bioconjugate chemistry · 2021Article
- Structure of a single-chain H2A/H2B dimer.Acta crystallographica. Section F, Structural biology communications · 2020Article
- AtFKBP53: a chimeric histone chaperone with functional nucleoplasmin and PPIase domains.Nucleic acids research · 2020Article
- Structure-function relationship of H2A-H2B specific plant histone chaperones.Cell stress & chaperones · 2020Review
- Nucleoplasmin is a limiting component in the scaling of nuclear size with cytoplasmic volume.The Journal of cell biology · 2019Article
- Newly developed Laboratory-based Size exclusion chromatography Small-angle x-ray scattering System (La-SSS).Scientific reports · 2019Article
- Review
- Structural insights into the ability of nucleoplasmin to assemble and chaperone histone octamers for DNA deposition.Scientific reports · 2019Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.