ArticleThe Journal of biological chemistry2012
Large multimeric assemblies of nucleosome assembly protein and histones revealed by small-angle X-ray scattering and electron microscopy.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Solution conformational differences between conventional and CENP-A nucleosomes are accentuated by reversible deformation under high pressure.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025Article
- Histone chaperone networks shaping chromatin function.Nature reviews. Molecular cell biology · 2017Review
- Coordinated Action of Nap1 and RSC in Disassembly of Tandem Nucleosomes.Molecular and cellular biology · 2016Article
- The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexes.Nucleic acids research · 2016Article
- Structural evidence for Nap1-dependent H2A-H2B deposition and nucleosome assembly.The EMBO journal · 2016Article
- The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution.Nucleic acids research · 2014Article
- Chaperones: needed for both the good times and the bad times.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Article
- Non-rigid image registration to reduce beam-induced blurring of cryo-electron microscopy images.Journal of synchrotron radiation · 2013Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The nucleosome assembly protein (NAP) family represents a key group of histone chaperones that are essential for cell viability. Several x-ray structures of NAP1 dimers are available; however, there are currently no structures of this ubiquitous chaperone in complex with histones. We have characterized NAP1 from Xenopus laevis and reveal that it forms discrete multimers with histones H2A/H2B and H3/H4 at a stoichiometry of one NAP dimer to one histone fold dimer. These complexes have been characterized by size exclusion chromatography, analytical ultracentrifugation, multiangle laser light scattering, and small-angle x-ray scattering to reveal their oligomeric assembly states in solution. By employing single-particle cryo-electron microscopy, we visualized these complexes for the first time and show that they form heterogeneous ring-like structures, potentially acting as large scaffolds for histone assembly and exchange.
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Registered trials
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