ArticlePLoS biology2019
Structural insights into histone chaperone Chz1-mediated H2A.Z recognition and histone replacement.
Article in PLoS biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 25 citations in OpenAlex.
- Histone Variant H2A.Z Enhances Histone and Nucleosome Dynamics.Molecular & cellular proteomics : MCP · 2026Article
- Structural and functional insights into the nuclear role of Parkinson's disease-associated α-synuclein as a histone chaperone.Communications biology · 2025Article
- Stabilization of the hexasome intermediate during histone exchange by yeast SWR1 complex.Molecular cell · 2024Article
- The SUN-family protein Sad1 mediates heterochromatin spatial organization through interaction with histone H2A-H2B.Nature communications · 2024Article
- Structural insights into histone exchange by human SRCAP complex.Cell discovery · 2024Article
- Article
- Epstein-Barr virus protein BKRF4 restricts nucleosome assembly to suppress host antiviral responses.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Chaperoning of the histone octamer by the acidic domain of DNA repair factor APLF.Science advances · 2022Article
- Coordinated DNA and histone dynamics drive accurate histone H2A.Z exchange.Science advances · 2022Article
- What makes a histone variant a variant: Changing H2A to become H2A.Z.PLoS genetics · 2021Article
- OsChz1 acts as a histone chaperone in modulating chromatin organization and genome function in rice.Nature communications · 2020Article
- Role of a DEF/Y motif in histone H2A-H2B recognition and nucleosome editing.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
Chz1 is a specific chaperone for the histone variant H2A.Z in budding yeast. The ternary complex formed by Chz1 and H2A.Z-H2B dimer is the major in vivo substrate of Swi2/snif2-related 1 (SWR1), the ATP-dependent chromatin remodeling enzyme that deposits H2A.Z into chromatin. However, the structural basis for the binding preference of Chz1 for H2A.Z over H2A and the mechanism by which Chz1 modulates the histone replacement remain elusive. Here, we show that Chz1 utilizes 2 distinct structural domains to engage the H2A.Z-H2B dimer for optimal and specific recognition of H2A.Z. The middle region of Chz1 (Chz1-M) directly interacts with 2 highly conserved H2A.Z-specific residues (Gly98 and Ala57) and dictates a modest preference for H2A.Z-H2B. In addition, structural and biochemical analysis show that the C-terminal region of Chz1 (Chz1-C) harbors a conserved DEF/Y motif, which reflects the consecutive D/E residues followed by a single aromatic residue, to engage an arginine finger and a hydrophobic pocket in H2A.Z-H2B, enhancing the binding preference for H2A.Z-H2B. Furthermore, Chz1 facilitates SWR1-mediated H2A.Z deposition by alleviating inhibition caused by aggregation of excess free histones, providing insights into how Chz1 controls the bioavailability of H2A.Z to assist SWR1 in promoter-specific installation of a histone mark. Our study elucidates a novel H2A.Z-recognition mechanism and uncovers a molecular rationale for binding of free histone by specialized histone chaperones in vivo.
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