ArticleProceedings of the National Academy of Sciences of the United States of America2010
Catalytic activation of histone acetyltransferase Rtt109 by a histone chaperone.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Epigenetic modulations in cancer: predictive biomarkers and potential targets for overcoming the resistance to topoisomerase I inhibitors.Annals of medicine · 2023Review
- Regulatory Roles of Histone Modifications in Filamentous Fungal Pathogens.Journal of fungi (Basel, Switzerland) · 2022Review
- Stoichiometry of Rtt109 complexes with Vps75 and histones H3-H4.Life science alliance · 2020Article
- Two factor authentication: Asf1 mediates crosstalk between H3 K14 and K56 acetylation.Nucleic acids research · 2019Article
- Histone chaperone exploits intrinsic disorder to switch acetylation specificity.Nature communications · 2019Article
- Metabonomics onEmerging microbes & infections · 2019Article
- Multisite Substrate Recognition in Asf1-Dependent Acetylation of Histone H3 K56 by Rtt109.Cell · 2018Article
- Structure-specific recognition protein-1 (SSRP1) is an elongated homodimer that binds histones.The Journal of biological chemistry · 2018Article
- Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation.Nucleic acids research · 2018Article
- Histone chaperone networks shaping chromatin function.Nature reviews. Molecular cell biology · 2017Review
- The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexes.Nucleic acids research · 2016Article
- The WOR1 5' untranslated region regulates white-opaque switching in Candida albicans by reducing translational efficiency.Molecular microbiology · 2015Article
- Histone exchange, chromatin structure and the regulation of transcription.Nature reviews. Molecular cell biology · 2015Review
- Article
- Cell cycle-dependent changes in H3K56ac in human cells.Cell cycle (Georgetown, Tex.) · 2015Article
- Writers and readers of histone acetylation: structure, mechanism, and inhibition.Cold Spring Harbor perspectives in biology · 2014Review
- The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution.Nucleic acids research · 2014Article
- Article
- The carboxyl terminus of Rtt109 functions in chaperone control of histone acetylation.Eukaryotic cell · 2013Article
- Chaperone-mediated acetylation of histones by Rtt109 identified by quantitative proteomics.Journal of proteomics · 2013Article
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Authors and funding
9 authors.
Funding
Abstract
Most histone acetyltransferases (HATs) function as multisubunit complexes in which accessory proteins regulate substrate specificity and catalytic efficiency. Rtt109 is a particularly interesting example of a HAT whose specificity and catalytic activity require association with either of two histone chaperones, Vps75 or Asf1. Here, we utilize biochemical, structural, and genetic analyses to provide the detailed molecular mechanism for activation of a HAT (Rtt109) by its activating subunit Vps75. The rate-determining step of the activated complex is the transfer of the acetyl group from acetyl CoA to the acceptor lysine residue. Vps75 stimulates catalysis (> 250-fold), not by contributing a catalytic base, but by stabilizing the catalytically active conformation of Rtt109. To provide structural insight into the functional complex, we produced a molecular model of Rtt109-Vps75 based on X-ray diffraction of crystals of the complex. This model reveals distinct negative electrostatic surfaces on an Rtt109 molecule that interface with complementary electropositive ends of a symmetrical Vps75 dimer. Rtt109 variants with interface point substitutions lack the ability to be fully activated by Vps75, and one such variant displayed impaired Vps75-dependent histone acetylation functions in yeast, yet these variants showed no adverse effect on Asf1-dependent Rtt109 activities in vitro and in vivo. Finally, we provide evidence for a molecular model in which a 12 complex of Rtt109-Vps75 acetylates a heterodimer of H3-H4. The activation mechanism of Rtt109-Vps75 provides a valuable framework for understanding the molecular regulation of HATs within multisubunit complexes.
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