ArticleScientific reports2017
Redundant Functions for Nap1 and Chz1 in H2A.Z Deposition.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Nucleosome Assembly Protein 1 in Dinoflagellate Cells Without Architectural Nucleosomes.International journal of molecular sciences · 2026Article
- Nap1 and Kap114 co-chaperone H2A-H2B and facilitate targeted histone release in the nucleus.The Journal of cell biology · 2025Article
- Chromatin balances cell redox and energy homeostasis.Epigenetics & chromatin · 2023Review
- Contribution of the histone variant H2A.Z to expression of responsive genes in plants.Seminars in cell & developmental biology · 2023Review
- What makes a histone variant a variant: Changing H2A to become H2A.Z.PLoS genetics · 2021Article
- The rDNA Loci-Intersections of Replication, Transcription, and Repair Pathways.International journal of molecular sciences · 2021Review
- OsChz1 acts as a histone chaperone in modulating chromatin organization and genome function in rice.Nature communications · 2020Article
- Epigenetic regulation: another layer in plant nutrition.Plant signaling & behavior · 2020Review
- Structural insights into histone chaperone Chz1-mediated H2A.Z recognition and histone replacement.PLoS biology · 2019Article
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Authors and funding
8 authors.
Funding
Abstract
H2A.Z is a histone H2A variant that contributes to transcriptional regulation, DNA damage response and limits heterochromatin spreading. In Saccharomyces cerevisiae, H2A.Z is deposited by the SWR-C complex, which relies on several histone chaperones including Nap1 and Chz1 to deliver H2A.Z-H2B dimers to SWR-C. However, the mechanisms by which Nap1 and Chz1 cooperate to bind H2A.Z and their contribution to H2A.Z deposition in chromatin is not well understood. Using structural modeling and molecular dynamics simulations, we identify a series of H2A.Z residues that form a chaperone-specific binding surface. Mutation of these residues revealed different surface requirements for Nap1 and Chz1 interaction with H2A.Z. Consistent with this result, we found that loss of Nap1 or Chz1 individually resulted in mild defects in H2A.Z deposition, but that deletion of both Nap1 and Chz1 resulted in a significant reduction of H2A.Z deposition at promoters and led to heterochromatin spreading. Together, our findings reveal unique H2A.Z surface dependences for Nap1 and Chz1 and a redundant role for these chaperones in H2A.Z deposition.
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