ArticleNucleic acids research2016
The histone chaperone sNASP binds a conserved peptide motif within the globular core of histone H3 through its TPR repeats.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- NASP functions in the cytoplasm to prevent histone H3 aggregation during early embryogenesis.The Journal of cell biology · 2026Article
- Chromatin adaptation and histone remodeling as mechanisms of PARP inhibitor resistance and therapeutic vulnerability.Frontiers in pharmacology · 2026Review
- NASP functions in the cytoplasm to prevent histone H3 aggregation during early embryogenesis.bioRxiv : the preprint server for biology · 2025Article
- The Chaperone NASP Contributes to de Novo Deposition of the Centromeric Histone Variant CENH3 in Arabidopsis Early Embryogenesis.Plant & cell physiology · 2024Article
- Ssn6 Interacts with Polar Tube Protein 2 and Transcriptional Repressor for RNA Polymerase II: Insight into Its Involvement in the Biological Process of MicrosporidiumJournal of fungi (Basel, Switzerland) · 2023Article
- Multilevel interrogation of H3.3 reveals a primordial role in transcription regulation.Epigenetics & chromatin · 2023Article
- DAXX adds a de novo H3.3K9me3 deposition pathway to the histone chaperone network.Molecular cell · 2023Article
- The Histone Chaperone Network Is Highly Conserved inInternational journal of molecular sciences · 2023Article
- A new route to the nucleus.eLife · 2022Article
- A specific role for importin-5 and NASP in the import and nuclear hand-off of monomeric H3.eLife · 2022Article
- The Role of the TSK/TONSL-H3.1 Pathway in Maintaining Genome Stability in Multicellular Eukaryotes.International journal of molecular sciences · 2022Review
- NASP maintains histone H3-H4 homeostasis through two distinct H3 binding modes.Nucleic acids research · 2022Article
- Article
- UBR7 acts as a histone chaperone for post-nucleosomal histone H3.The EMBO journal · 2021Article
- Distinct histone H3-H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones.Genes & development · 2021Article
- Chasing Tails: Cathepsin-L Improves Structural Analysis of Histones by HX-MS.Molecular & cellular proteomics : MCP · 2019Article
- The histone chaperoning pathway: from ribosome to nucleosome.Essays in biochemistry · 2019Review
- Evidence for the nuclear import of histones H3.1 and H4 as monomers.The EMBO journal · 2018Article
- CHD3 and CHD4 recruitment and chromatin remodeling activity at DNA breaks is promoted by early poly(ADP-ribose)-dependent chromatin relaxation.Nucleic acids research · 2018Article
- Functional Analysis of Hif1 Histone Chaperone inG3 (Bethesda, Md.) · 2018Article
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7 authors.
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Abstract
Eukaryotic chromatin is a complex yet dynamic structure, which is regulated in part by the assembly and disassembly of nucleosomes. Key to this process is a group of proteins termed histone chaperones that guide the thermodynamic assembly of nucleosomes by interacting with soluble histones. Here we investigate the interaction between the histone chaperone sNASP and its histone H3 substrate. We find that sNASP binds with nanomolar affinity to a conserved heptapeptide motif in the globular domain of H3, close to the C-terminus. Through functional analysis of sNASP homologues we identified point mutations in surface residues within the TPR domain of sNASP that disrupt H3 peptide interaction, but do not completely disrupt binding to full length H3 in cells, suggesting that sNASP interacts with H3 through additional contacts. Furthermore, chemical shift perturbations from(1)H-(15)N HSQC experiments show that H3 peptide binding maps to the helical groove formed by the stacked TPR motifs of sNASP. Our findings reveal a new mode of interaction between a TPR repeat domain and an evolutionarily conserved peptide motif found in canonical H3 and in all histone H3 variants, including CenpA and have implications for the mechanism of histone chaperoning within the cell.
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