ArticleNucleic acids research2012
The human histone chaperone sNASP interacts with linker and core histones through distinct mechanisms.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Mind the gap: Epigenetic regulation of chromatin accessibility in plants.Plant physiology · 2024Review
- The Histone Chaperone Network Is Highly Conserved inInternational journal of molecular sciences · 2023Article
- NASP maintains histone H3-H4 homeostasis through two distinct H3 binding modes.Nucleic acids research · 2022Article
- Article
- Distinct histone H3-H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones.Genes & development · 2021Article
- The histone chaperone Nrp1 is required for chromatin stability and nuclear division in Tetrahymena thermophila.Epigenetics & chromatin · 2021Article
- Histone acetyltransferase 1 is required for DNA replication fork function and stability.The Journal of biological chemistry · 2020Article
- Nucleus-specific linker histones Hho1 and Mlh1 form distinct protein interactions during growth, starvation and development in Tetrahymena thermophila.Scientific reports · 2020Article
- Functional Proteomics of Nuclear Proteins inGenes · 2019Review
- Functional Analysis of Hif1 Histone Chaperone inG3 (Bethesda, Md.) · 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
- sNASP and ASF1A function through both competitive and compatible modes of histone binding.Nucleic acids research · 2017Article
- Identification of replication-dependent and replication-independent linker histone complexes: Tpr specifically promotes replication-dependent linker histone stability.BMC biochemistry · 2016Article
- The histone chaperone sNASP binds a conserved peptide motif within the globular core of histone H3 through its TPR repeats.Nucleic acids research · 2016Article
- Single-Molecule Studies of the Linker Histone H1 Binding to DNA and the Nucleosome.Biochemistry · 2016Article
- Glutamylation of Nap1 modulates histone H1 dynamics and chromosome condensation in Xenopus.The Journal of cell biology · 2015Article
- Molecular evolution of NASP and conserved histone H3/H4 transport pathway.BMC evolutionary biology · 2014Article
- Article
- H1 histones: current perspectives and challenges.Nucleic acids research · 2013Review
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Authors and funding
4 authors.
Funding
Abstract
Somatic nuclear autoantigenic sperm protein (sNASP) is a human homolog of the N1/N2 family of histone chaperones. sNASP contains the domain structure characteristic of this family, which includes a large acidic patch flanked by several tetratricopeptide repeat (TPR) motifs. sNASP possesses a unique binding specificity in that it forms specific complexes with both histone H1 and histones H3/H4. Based on the binding affinities of sNASP variants to histones H1, H3.3, H4 and H3.3/H4 complexes, sNASP uses distinct structural domains to interact with linker and core histones. For example, one of the acidic patches of sNASP was essential for linker histone binding but not for core histone interactions. The fourth TPR of sNASP played a critical role in interactions with histone H3/H4 complexes, but did not influence histone H1 binding. Finally, analysis of cellular proteins demonstrated that sNASP existed in distinct complexes that contained either linker or core histones.
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