ArticleGenetics2008
Catalytic-site mutations in the MYST family histone Acetyltransferase Esa1.
Article in Genetics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
26 citing papers in PubMed, 39 citations in OpenAlex.
- TIP60 acts as a wound-induced factor essential for efficient regeneration in planaria.The Journal of biological chemistry · 2026Article
- Review
- Histone acetyltransferase Sas3 contributes to fungal development, cell wall integrity, and virulence inApplied and environmental microbiology · 2024Article
- Crotonylation modification and its role in diseases.Frontiers in molecular biosciences · 2024Review
- Chromodomain mutation in S. pombe Kat5/Mst1 affects centromere dynamics and DNA repair.PloS one · 2024Article
- Article
- A Saccharomyces cerevisiae model and screen to define the functional consequences of oncogenic histone missense mutations.G3 (Bethesda, Md.) · 2022Article
- Protein lysine crotonylation: past, present, perspective.Cell death & disease · 2021Review
- Gcn5 and Esa1 function as histone crotonyltransferases to regulate crotonylation-dependent transcription.The Journal of biological chemistry · 2019Article
- NuA4 acetyltransferase is required for efficient nucleotide excision repair in yeast.DNA repair · 2019Article
- Article
- MOF as an evolutionarily conserved histone crotonyltransferase and transcriptional activation by histone acetyltransferase-deficient and crotonyltransferase-competent CBP/p300.Cell discovery · 2017Article
- Intrinsic ubiquitin E3 ligase activity of histone acetyltransferase Hbo1 for estrogen receptor α.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2017Article
- Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT).International journal of molecular sciences · 2016Review
- Article
- The microtubule-associated tau protein has intrinsic acetyltransferase activity.Nature structural & molecular biology · 2013Article
- mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Piccolo NuA4-catalyzed acetylation of nucleosomal histones: critical roles of an Esa1 Tudor/chromo barrel loop and an Epl1 enhancer of polycomb A (EPcA) basic region.Molecular and cellular biology · 2013Article
- Suppression analysis of esa1 mutants in Saccharomyces cerevisiae links NAB3 to transcriptional silencing and nucleolar functions.G3 (Bethesda, Md.) · 2012Article
- Implication of posttranslational histone modifications in nucleotide excision repair.International journal of molecular sciences · 2012Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Esa1 is the only essential histone acetyltransferase (HAT) in budding yeast. It is the catalytic subunit of at least two multiprotein complexes, NuA4 and Piccolo NuA4 (picNuA4), and its essential function is believed to be its catalytic HAT activity. To examine the role of Esa1 in DNA damage repair, we isolated viable esa1 mutants with a range of hypersensitivities to the toposide camptothecin. Here we show that the sensitivity of these mutants to a variety of stresses is inversely proportional to their level of histone H4 acetylation, demonstrating the importance of Esa1 catalytic activity for resistance to genotoxic stress. Surprisingly, individual mutations in two residues directly involved in catalysis were not lethal even though the mutant enzymes appear catalytically inactive both in vivo and in vitro. However, the double-point mutant is lethal, demonstrating that the essential function of Esa1 relies on residues within the catalytic pocket but not catalysis. We propose that the essential function of Esa1 may be to bind acetyl-CoA or lysine substrates and positively regulate the activities of NuA4 and Piccolo NuA4.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.