ArticleProceedings of the National Academy of Sciences of the United States of America1999
Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.
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Who cites it
84 citing papers in PubMed, 182 citations in OpenAlex.
- Mechanistic insights into histone recognition and H3K14 acetylation by the NuA3 histone acetyltransferase complex.Nature communications · 2025Article
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- Structure-function analysis of carrier protein-dependent 2-sulfamoylacetyl transferase in the biosynthesis of altemicidin.Nature communications · 2024Article
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- Histone acetyltransferase Gcn5-mediated histone H3 acetylation facilitates cryptococcal morphogenesis and sexual reproduction.mSphere · 2023Article
- Epigenetic moonlighting: Catalytic-independent functions of histone modifiers in regulating transcription.Science advances · 2023Review
- Highlighting the Unique Roles of RadicalJournal of bacteriology · 2022Review
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- The Ada2/Ada3/Gcn5/Sgf29 histone acetyltransferase module.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021Review
- Catalysis by protein acetyltransferase Gcn5.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021Review
- Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates.Nature communications · 2020Article
- The Elongator subunit Elp3 is a non-canonical tRNA acetyltransferase.Nature communications · 2019Article
- Post-translational Protein Acetylation: An Elegant Mechanism for Bacteria to Dynamically Regulate Metabolic Functions.Frontiers in microbiology · 2019Review
- lncRNA GCAWKR Promotes Gastric Cancer Development by Scaffolding the Chromatin Modification Factors WDR5 and KAT2A.Molecular therapy : the journal of the American Society of Gene Therapy · 2018Article
- Structural basis for activation of SAGA histone acetyltransferase Gcn5 by partner subunit Ada2.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Convergent microevolution of Cryptococcus neoformans hypervirulence in the laboratory and the clinic.Scientific reports · 2017Article
- Enoyl-CoA hydratase-1 regulates mTOR signaling and apoptosis by sensing nutrients.Nature communications · 2017Article
- Acetylation- and Methylation-Related Epigenetic Proteins in the Context of Their Targets.Genes · 2017Review
- Discovering Targets of Non-enzymatic Acylation by Thioester Reactivity Profiling.Cell chemical biology · 2017Article
- Recognition of ubiquitinated nucleosomes.Current opinion in structural biology · 2017Review
24 more citing papers are in PubMed but not listed here.
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9 authors at 3 institutions in 1 country.
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Abstract
The yeast GCN5 (yGCN5) transcriptional coactivator functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Here, we present the high resolution crystal structure of the HAT domain of yGCN5 and probe the functional importance of a conserved glutamate residue. The structure reveals a central protein core associated with AcCoA binding that appears to be structurally conserved among a superfamily of N-acetyltransferases, including yeast histone acetyltransferase 1 and Serratia marcescens aminoglycoside 3-N-acetyltransferase. A pronounced cleft lying above this core, and flanked by N- and C-terminal regions that show no sequence conservation within N-acetyltransferase enzymes, is implicated by cross-species conservation and mutagenesis studies to be a site for histone substrate binding and catalysis. Located at the bottom of this cleft is a conserved glutamate residue (E173) that is in position to play an important catalytic role in histone acetylation. Functional analysis of an E173Q mutant yGCN5 protein implicates glutamate 173 to function as a general base for catalysis. Together, a correlation of the yGCN5 structure with functionally debilitating yGCN5 mutations provides a paradigm for understanding the structure/function relationships of the growing number of transcriptional regulators that function as histone acetyltransferase enzymes.
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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.