ArticleJournal of molecular biology2008
A beta-hairpin comprising the nuclear localization sequence sustains the self-associated states of nucleosome assembly protein 1.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 45 citations in OpenAlex.
- Nucleosome Assembly Protein 1 in Dinoflagellate Cells Without Architectural Nucleosomes.International journal of molecular sciences · 2026Article
- Structural basis for HIV-1 Rev recognition by the histone chaperone human Nap1.The Journal of biological chemistry · 2026Article
- Nap1 and Kap114 co-chaperone H2A-H2B and facilitate targeted histone release in the nucleus.The Journal of cell biology · 2025Article
- Histone chaperone Nap1 dismantles an H2A/H2B dimer from a partially unwrapped nucleosome.Nucleic acids research · 2023Article
- Structural comparisons reveal diverse binding modes between nucleosome assembly proteins and histones.Epigenetics & chromatin · 2022Review
- NAP1L1 and NAP1L4 Binding to Hypervariable Domain of Chikungunya Virus nsP3 Protein Is Bivalent and Requires Phosphorylation.Journal of virology · 2021Article
- Analytical Ultracentrifugation (AUC): An Overview of the Application of Fluorescence and Absorbance AUC to the Study of Biological Macromolecules.Current protocols in molecular biology · 2020Article
- Comprehensive analysis of histone-binding proteins with multi-angle light scattering.Methods (San Diego, Calif.) · 2020Article
- Structure-function relationship of H2A-H2B specific plant histone chaperones.Cell stress & chaperones · 2020Review
- Multiple Host Factors Interact with the Hypervariable Domain of Chikungunya Virus nsP3 and Determine Viral Replication in Cell-Specific Mode.Journal of virology · 2018Article
- 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
- Large multimeric assemblies of nucleosome assembly protein and histones revealed by small-angle X-ray scattering and electron microscopy.The Journal of biological chemistry · 2012Article
- Histone chaperones link histone nuclear import and chromatin assembly.Biochimica et biophysica acta · 2012Article
- The histone chaperones Nap1 and Vps75 bind histones H3 and H4 in a tetrameric conformation.Molecular cell · 2011Article
- Structure and Scm3-mediated assembly of budding yeast centromeric nucleosomes.Nature communications · 2011Article
- The histone shuffle: histone chaperones in an energetic dance.Trends in biochemical sciences · 2010Review
- Histone chaperones, histone acetylation, and the fluidity of the chromogenome.Journal of cellular physiology · 2010Article
- A thermodynamic model for Nap1-histone interactions.The Journal of biological chemistry · 2008Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The histone chaperone nucleosome assembly protein 1 (NAP1) is implicated in histone shuttling as well as nucleosome assembly and disassembly. Under physiological conditions, NAP1 dimers exist in a mixture of various high-molecular-weight oligomers whose size may be regulated by the cell cycle-dependent concentration of NAP1. Both the functional and structural significance of the observed oligomers are unknown. We have resolved the molecular mechanism by which yeast NAP1 (yNAP1) dimers oligomerize by applying x-ray crystallographic, hydrodynamic, and functional approaches. We found that an extended beta-hairpin that protrudes from the compact core of the yNAP1 dimer forms a stable beta-sheet with beta-hairpins of neighboring yNAP1 dimers. Disruption of the beta-hairpin (whose sequence is conserved among NAP1 proteins in various species) by the replacement of one or more amino acids with proline results in complete loss of yNAP1 dimer oligomerization. The in vitro functions of yNAP1 remain unaffected by the mutations. We have thus identified a conserved structural feature of NAP1 whose function, in addition to presenting the nuclear localization sequence, appears to be the formation of higher-order oligomers.
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Registered trials
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.