ArticleGenes & development2014
Hat2p recognizes the histone H3 tail to specify the acetylation of the newly synthesized H3/H4 heterodimer by the Hat1p/Hat2p complex.
Article in Genes & development, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 36 citations in OpenAlex.
- A specific role for importin-5 and NASP in the import and nuclear hand-off of monomeric H3.eLife · 2022Article
- Topography of histone H3-H4 interaction with the Hat1-Hat2 acetyltransferase complex.Genes & development · 2022Article
- Epigenetic regulation of nuclear lamina-associated heterochromatin by HAT1 and the acetylation of newly synthesized histones.Nucleic acids research · 2021Article
- Distinct histone H3-H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones.Genes & development · 2021Article
- RbAp46/48LIN-53 and HAT-1 are required for initial CENP-AHCP-3 deposition and de novo holocentromere formation on artificial chromosomes in Caenorhabditis elegans embryos.Nucleic acids research · 2021Article
- InterPep2: global peptide-protein docking using interaction surface templates.Bioinformatics (Oxford, England) · 2020Article
- The histone chaperoning pathway: from ribosome to nucleosome.Essays in biochemistry · 2019Review
- Histones H3 and H4 require their relevant amino-tails for efficient nuclear import and replication-coupled chromatin assembly in vivo.Scientific reports · 2017Article
- Structural and mechanistic insights into regulation of HBO1 histone acetyltransferase activity by BRPF2.Nucleic acids research · 2017Article
- Histone chaperone networks shaping chromatin function.Nature reviews. Molecular cell biology · 2017Review
- sNASP and ASF1A function through both competitive and compatible modes of histone binding.Nucleic acids research · 2017Article
- Recognition Elements in the Histone H3 and H4 Tails for Seven Different Importins.The Journal of biological chemistry · 2016Article
- Structural and Functional Role of Acetyltransferase hMOF K274 Autoacetylation.The Journal of biological chemistry · 2016Article
- Structure and function of human Naa60 (NatF), a Golgi-localized bi-functional acetyltransferase.Scientific reports · 2016Article
- The histone chaperone sNASP binds a conserved peptide motif within the globular core of histone H3 through its TPR repeats.Nucleic acids research · 2016Article
- Molecular Basis for Histone Acetyltransferase Regulation by Binding Partners, Associated Domains, and Autoacetylation.ACS chemical biology · 2016Review
- The N-terminal Acetyltransferase Naa10/ARD1 Does Not Acetylate Lysine Residues.The Journal of biological chemistry · 2016Article
- Dissecting the Molecular Roles of Histone Chaperones in Histone Acetylation by Type B Histone Acetyltransferases (HAT-B).The Journal of biological chemistry · 2015Article
- Article
- The molecular basis for histone H4- and H2A-specific amino-terminal acetylation by NatD.Structure (London, England : 1993) · 2015Article
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Authors and funding
15 authors at 6 institutions in 2 countries.
Funding
Abstract
Post-translational modifications of histones are significant regulators of replication, transcription, and DNA repair. Particularly, newly synthesized histone H4 in H3/H4 heterodimers becomes acetylated on N-terminal lysine residues prior to its incorporation into chromatin. Previous studies have established that the histone acetyltransferase (HAT) complex Hat1p/Hat2p medicates this modification. However, the mechanism of how Hat1p/Hat2p recognizes and facilitates the enzymatic activities on the newly assembled H3/H4 heterodimer remains unknown. Furthermore, Hat2p is a WD40 repeat protein, which is found in many histone modifier complexes. However, how the WD40 repeat proteins facilitate enzymatic activities of histone modification enzymes is unclear. In this study, we first solved the high-resolution crystal structure of a Hat1p/Hat2p/CoA/H4 peptide complex and found that the H4 tail interacts with both Hat1p and Hat2p, by which substrate recruitment is facilitated. We further discovered that H3 N-terminal peptides can bind to the Hat2p WD40 domain and solved the structure of the Hat1p/Hat2p/CoA/H4/H3 peptide complex. Moreover, the interaction with Hat2p requires unmodified Arg2/Lys4 and Lys9 on the H3 tail, suggesting a novel model to specify the activity of Hat1p/Hat2p toward newly synthesized H3/H4 heterodimers. Together, our study demonstrated the substrate recognition mechanism by the Hat1p/Hat2p complex, which is critical for DNA replication and other chromatin remodeling processes.
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