ArticleEukaryotic cell2006
Pair of unusual GCN5 histone acetyltransferases and ADA2 homologues in the protozoan parasite Toxoplasma gondii.
Article in Eukaryotic cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 60 citations in OpenAlex.
- Profile of lysine acetylation in Eimeria tenella and its potential implications for anticoccidial research.Parasites & vectors · 2026Article
- A role for the poly-asparagine repeat in the Plasmodium histone acetyltransferase, PfGCN5.Nature communications · 2026Article
- Article
- Analysis of the role of acetylation inFrontiers in microbiology · 2024Article
- The multifaceted roles of Myb domain-containing proteins in apicomplexan parasites.Current opinion in microbiology · 2023Review
- Article
- Advances in Protozoan Epigenetic Targets and Their Inhibitors for the Development of New Potential Drugs.Pharmaceuticals (Basel, Switzerland) · 2023Review
- Previously Unidentified Histone H1-Like Protein Is Involved in Cell Division and Ribosome Biosynthesis in Toxoplasma gondii.mSphere · 2022Article
- "Reading" a new chapter in protozoan parasite transcriptional regulation.PLoS pathogens · 2021Review
- Lysine crotonylation is widespread on proteins of diverse functions and localizations in Toxoplasma gondii.Parasitology research · 2021Article
- Evaluating the GCN5b bromodomain as a novel therapeutic target against the parasite Toxoplasma gondii.Experimental parasitology · 2020Article
- A novel GCN5b lysine acetyltransferase complex associates with distinct transcription factors in the protozoan parasite Toxoplasma gondii.Molecular and biochemical parasitology · 2019Article
- A latent ability to persist: differentiation in Toxoplasma gondii.Cellular and molecular life sciences : CMLS · 2018Review
- The Apicomplexa-specific glucosamine-6-phosphate N-acetyltransferase gene family encodes a key enzyme for glycoconjugate synthesis with potential as therapeutic target.Scientific reports · 2018Article
- Article
- Bromodomains in Protozoan Parasites: Evolution, Function, and Opportunities for Drug Development.Microbiology and molecular biology reviews : MMBR · 2017Review
- O-fucosylated glycoproteins form assemblies in close proximity to the nuclear pore complexes of Toxoplasma gondii.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Garcinol Inhibits GCN5-Mediated Lysine Acetyltransferase Activity and Prevents Replication of the Parasite Toxoplasma gondii.Antimicrobial agents and chemotherapy · 2016Article
- The Knowns Unknowns: Exploring the Homologous Recombination Repair Pathway in Toxoplasma gondii.Frontiers in microbiology · 2016Review
- HAT3-mediated acetylation of PCNA precedes PCNA monoubiquitination following exposure to UV radiation in Leishmania donovani.Nucleic acids research · 2015Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
GCN5 is a histone acetyltransferase (HAT) essential for development in mammals and critical to stress responses in yeast. The protozoan parasite Toxoplasma gondii is a serious opportunistic pathogen. The study of epigenetics and gene expression in this ancient eukaryote has pharmacological relevance and may facilitate the understanding of these processes in higher eukaryotes. Here we show that the disruption of T. gondii GCN5 yields viable parasites, which were subsequently employed in a proteomics study to identify gene products affected by its loss. Promoter analysis of these TgGCN5-dependent genes, which were mostly parasite specific, reveals a conserved T-rich element. The loss of TgGCN5 does not attenuate virulence in an in vivo mouse model. We also discovered that T. gondii is the only invertebrate reported to date possessing a second GCN5 (TgGCN5-B). TgGCN5-B harbors a strikingly divergent N-terminal domain required for nuclear localization. Despite high homology between the HAT domains, the two TgGCN5s exhibit differing substrate specificities. In contrast to TgGCN5-A, which exclusively targets lysine 18 of H3, TgGCN5-B acetylates multiple lysines in the H3 tail. We also identify two ADA2 homologues that interact differently with the TgGCN5s. TgGCN5-B has the potential to compensate for TgGCN5-A, which probably arose from a gene duplication unique to T. gondii. Our work reveals an unexpected complexity in the GCN5 machinery of this primitive eukaryote.
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