ArticleNature communications2019
Histone chaperone exploits intrinsic disorder to switch acetylation specificity.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 30 citations in OpenAlex.
- Connected Chromatin Amplifies Acetylation-Modulated Nucleosome Interactions.Biochemistry · 2025Article
- Driving forces of the complex formation between highly charged disordered proteins.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The EJC disassembly factor PYM is an intrinsically disordered protein and forms a fuzzy complex with RNA.Frontiers in molecular biosciences · 2023Article
- Affinity of disordered protein complexes is modulated by entropy-energy reinforcement.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Combining histone deacetylase inhibitors (HDACis) with other therapies for cancer therapy.European journal of medicinal chemistry · 2021Review
- Arsenic-induced epigenetic changes in cancer development.Seminars in cancer biology · 2021Review
- NMR illuminates intrinsic disorder.Current opinion in structural biology · 2021Review
- Histone Tail Conformations: A Fuzzy Affair with DNA.Trends in biochemical sciences · 2021Review
- Evolutionary crossroads of cell signaling: PP1 and PP2A substrate sites in intrinsically disordered regions.Biochemical Society transactions · 2021Review
- Histone tails as signaling antennas of chromatin.Current opinion in structural biology · 2021Review
- Heritable pattern of oxidized DNA base repair coincides with pre-targeting of repair complexes to open chromatin.Nucleic acids research · 2021Article
- Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes.Nature communications · 2020Article
- Stoichiometry of Rtt109 complexes with Vps75 and histones H3-H4.Life science alliance · 2020Article
- Structure of a Protein-RNA Complex by Solid-State NMR Spectroscopy.Angewandte Chemie (International ed. in English) · 2020Article
- NMR Methods for Structural Characterization of Protein-Protein Complexes.Frontiers in molecular biosciences · 2020Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Histones, the principal protein components of chromatin, contain long disordered sequences, which are extensively post-translationally modified. Although histone chaperones are known to control both the activity and specificity of histone-modifying enzymes, the mechanisms promoting modification of highly disordered substrates, such as lysine-acetylation within the N-terminal tail of histone H3, are not understood. Here, to understand how histone chaperones Asf1 and Vps75 together promote H3 K9-acetylation, we establish the solution structural model of the acetyltransferase Rtt109 in complex with Asf1 and Vps75 and the histone dimer H3:H4. We show that Vps75 promotes K9-acetylation by engaging the H3 N-terminal tail in fuzzy electrostatic interactions with its disordered C-terminal domain, thereby confining the H3 tail to a wide central cavity faced by the Rtt109 active site. These fuzzy interactions between disordered domains achieve localization of lysine residues in the H3 tail to the catalytic site with minimal loss of entropy, and may represent a common mechanism of enzymatic reactions involving highly disordered substrates.
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