ArticleThe Journal of biological chemistry2011
Nuclear Hat1p complex (NuB4) components participate in DNA repair-linked chromatin reassembly.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Histone Acetylation Landscape and the Role of HAT1 in Regulating Corneal Epithelial Wound Healing.Investigative ophthalmology & visual science · 2026Article
- RebL1 is required for macronuclear structure stability and gametogenesis inMarine life science & technology · 2024Article
- The Role of Chromatin Assembly Factors in Induced Mutagenesis at Low Levels of DNA Damage.Genes · 2023Article
- Understanding HAT1: A Comprehensive Review of Noncanonical Roles and Connection with Disease.Genes · 2023Review
- Article
- Metabolomic and Proteomic Changes inInternational journal of molecular sciences · 2022Article
- Article
- Hat1-Dependent Lysine Acetylation Targets Diverse Cellular Functions.Journal of proteome research · 2020Article
- Early-onset aging and mitochondrial defects associated with loss of histone acetyltransferase 1 (Hat1).Aging cell · 2019Article
- Functional Analysis of Hif1 Histone Chaperone inG3 (Bethesda, Md.) · 2018Article
- Identification of multiple roles for histone acetyltransferase 1 in replication-coupled chromatin assembly.Nucleic acids research · 2017Article
- KATapulting toward Pluripotency and Cancer.Journal of molecular biology · 2017Review
- Identification of replication-dependent and replication-independent linker histone complexes: Tpr specifically promotes replication-dependent linker histone stability.BMC biochemistry · 2016Article
- Molecular Basis for Histone Acetyltransferase Regulation by Binding Partners, Associated Domains, and Autoacetylation.ACS chemical biology · 2016Review
- Dissecting the Molecular Roles of Histone Chaperones in Histone Acetylation by Type B Histone Acetyltransferases (HAT-B).The Journal of biological chemistry · 2015Article
- The Candida albicans Histone Acetyltransferase Hat1 Regulates Stress Resistance and Virulence via Distinct Chromatin Assembly Pathways.PLoS pathogens · 2015Article
- Hat2p recognizes the histone H3 tail to specify the acetylation of the newly synthesized H3/H4 heterodimer by the Hat1p/Hat2p complex.Genes & development · 2014Article
- RNAi screening identifies HAT1 as a potential drug target in esophageal squamous cell carcinoma.International journal of clinical and experimental pathology · 2014Article
- Article
- Sites of acetylation on newly synthesized histone H4 are required for chromatin assembly and DNA damage response signaling.Molecular and cellular biology · 2013Article
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Authors and funding
3 authors.
Funding
Abstract
Chromatin is disassembled and reassembled during DNA repair. To assay chromatin reassembly accompanying DNA double strand break repair, ChIP analysis can be used to monitor the presence of histone H3 near the lesion. The chromatin assembly factor Asf1p, as well as the acetylation of histone H3 lysine 56, have been shown to promote chromatin reassembly when DNA double strand break repair is complete. Using Gal-HO-mediated double strand break repair, we have tested each of the components of the nuclear Hat1p-containing type B histone acetyltransferase complex (NuB4) and have found that they can affect repair-linked chromatin reassembly but that their contributions are not equivalent. In particular, deletion of the catalytic subunit, Hat1p, caused a significant defect in chromatin reassembly. In addition, loss of the histone chaperone Hif1p, when combined with an allele of H3 that mutates lysines 14 and 23 to arginine, has a pronounced effect on chromatin reassembly that is similar to that observed in an asf1Δ. The role of Hat1p and Hif1p is at least partially redundant with the role of Asf1p. Consistent with a more prominent role for Hif1p in chromatin reassembly than either Hat1p or Hat2p, Hif1p exists in complex(es) independent of Hat1p and Hat2p and influences the activity of an H3-specific histone acetyltransferase activity. Our data directly demonstrate the role of the nuclear HAT1 complex (NuB4) components in DNA repair-linked chromatin reassembly.
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