ArticleNucleic acids research2017
sNASP and ASF1A function through both competitive and compatible modes of histone binding.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 34 citations in OpenAlex.
- Arabidopsis histone acetyltransferase complex coordinates cytoplasmic histone acetylation and nuclear chromatin accessibility.Science advances · 2024Article
- The Chaperone NASP Contributes to de Novo Deposition of the Centromeric Histone Variant CENH3 in Arabidopsis Early Embryogenesis.Plant & cell physiology · 2024Article
- 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 specific role for importin-5 and NASP in the import and nuclear hand-off of monomeric H3.eLife · 2022Article
- NASP maintains histone H3-H4 homeostasis through two distinct H3 binding modes.Nucleic acids research · 2022Article
- 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
- Monobodies as tool biologics for accelerating target validation and druggable site discovery.RSC medicinal chemistry · 2021Review
- DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network.Molecular cell · 2021Article
- CAF-1 and Rtt101p function within the replication-coupled chromatin assembly network to promote H4 K16ac, preventing ectopic silencing.PLoS genetics · 2020Article
- Interactions With Histone H3 & Tools to Study Them.Frontiers in cell and developmental biology · 2020Review
- 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
- Functional Analysis of Hif1 Histone Chaperone inG3 (Bethesda, Md.) · 2018Article
- Copy number variants in Ebstein anomaly.PloS one · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
Histone chaperones are proteins that interact with histones to regulate the thermodynamic process of nucleosome assembly. sNASP and ASF1 are conserved histone chaperones that interact with histones H3 and H4 and are found in a multi-chaperoning complex in vivo Previously we identified a short peptide motif within H3 that binds to the TPR domain of sNASP with nanomolar affinity. Interestingly, this peptide motif is sequestered within the known ASF1-H3-H4 interface, raising the question of how these two proteins are found in complex together with histones when they share the same binding site. Here, we show that sNASP contains at least two additional histone interaction sites that, unlike the TPR-H3 peptide interaction, are compatible with ASF1A binding. These surfaces allow ASF1A to form a quaternary complex with both sNASP and H3-H4. Furthermore, we demonstrate that sNASP makes a specific complex with H3 on its own in vitro, but not with H4, suggesting that it could work upstream of ASF1A. Further, we show that sNASP and ASF1A are capable of folding an H3-H4 dimer in vitro under native conditions. These findings reveal a network of binding events that may promote the entry of histones H3 and H4 into the nucleosome assembly pathway.
Indexed as
Identifiers
What OpenQuestion holds
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.