ArticleScientific reports2016
A Quantitative Characterization of Nucleoplasmin/Histone Complexes Reveals Chaperone Versatility.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Identification of target cells of human papillomavirus 18 using squamocolumnar junction organoids.Cancer science · 2024Article
- Plant-specific HDT family histone deacetylases are nucleoplasmins.The Plant cell · 2022Article
- Histone Chaperones as Cardinal Players in Development.Frontiers in cell and developmental biology · 2022Review
- AtFKBP53: a chimeric histone chaperone with functional nucleoplasmin and PPIase domains.Nucleic acids research · 2020Article
- Structural insights into the ability of nucleoplasmin to assemble and chaperone histone octamers for DNA deposition.Scientific reports · 2019Article
- Chaperones and Beyond as Key Players in Pluripotency Maintenance.Frontiers in cell and developmental biology · 2019Review
- Double maternal-effect: duplicated nucleoplasmin 2 genes, npm2a and npm2b, with essential but distinct functions are shared by fish and tetrapods.BMC evolutionary biology · 2018Article
- Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release.Nature communications · 2017Article
- Fly Fishing for Histones: Catch and Release by Histone Chaperone Intrinsically Disordered Regions and Acidic Stretches.Journal of molecular biology · 2017Review
- Chromosomal passenger complex hydrodynamics suggests chaperoning of the inactive state by nucleoplasmin/nucleophosmin.Molecular biology of the cell · 2017Article
- Histone chaperone networks shaping chromatin function.Nature reviews. Molecular cell biology · 2017Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nucleoplasmin (NP) is an abundant histone chaperone in vertebrate oocytes and embryos involved in storing and releasing maternal histones to establish and maintain the zygotic epigenome. NP has been considered a H2A-H2B histone chaperone, and recently it has been shown that it can also interact with H3-H4. However, its interaction with different types of histones has not been quantitatively studied so far. We show here that NP binds H2A-H2B, H3-H4 and linker histones with Kd values in the subnanomolar range, forming different complexes. Post-translational modifications of NP regulate exposure of the polyGlu tract at the disordered distal face of the protein and induce an increase in chaperone affinity for all histones. The relative affinity of NP for H2A-H2B and linker histones and the fact that they interact with the distal face of the chaperone could explain their competition for chaperone binding, a relevant process in NP-mediated sperm chromatin remodelling during fertilization. Our data show that NP binds H3-H4 tetramers in a nucleosomal conformation and dimers, transferring them to DNA to form disomes and tetrasomes. This finding might be relevant to elucidate the role of NP in chromatin disassembly and assembly during replication and transcription.
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