ArticlePloS one2013
Comprehensive histone phosphorylation analysis and identification of Pf14-3-3 protein as a histone H3 phosphorylation reader in malaria parasites.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 44 citations in OpenAlex.
- PfPPM2 signalling regulates asexual division and sexual conversion of human malaria parasite Plasmodium falciparum.Nature communications · 2025Article
- Enrichment of H3S28p and H3K9me2 Epigenetic Marks on Inflammatory-Associated Gene Promoters in Response to Severe Burn Injury.Life (Basel, Switzerland) · 2024Article
- Hungry for control: metabolite signaling to chromatin in Plasmodium falciparum.Current opinion in microbiology · 2024Review
- Epigenetic regulation as a therapeutic target in the malaria parasite Plasmodium falciparum.Malaria journal · 2024Review
- The Nitrobenzoxadiazole Derivative NBDHEX Behaves asPharmaceuticals (Basel, Switzerland) · 2022Article
- Histone Modification Landscapes as a Roadmap for Malaria Parasite Development.Frontiers in cell and developmental biology · 2022Review
- "Reading" a new chapter in protozoan parasite transcriptional regulation.PLoS pathogens · 2021Review
- A unique GCN5 histone acetyltransferase complex controls erythrocyte invasion and virulence in the malaria parasite Plasmodium falciparum.PLoS pathogens · 2021Article
- A novel heteromeric pantothenate kinase complex in apicomplexan parasites.PLoS pathogens · 2021Article
- The ApiAP2 factor PfAP2-HC is an integral component of heterochromatin in the malaria parasiteiScience · 2021Article
- Novel insights from the Plasmodium falciparum sporozoite-specific proteome by probabilistic integration of 26 studies.PLoS computational biology · 2021Article
- Phosphorylation of the Canonical Histone H2A Marks Foci of Damaged DNA in Malaria Parasites.mSphere · 2021Article
- Epigenetic reader complexes of the human malaria parasite, Plasmodium falciparum.Nucleic acids research · 2019Article
- Clipped histone H3 is integrated into nucleosomes of DNA replication genes in the human malaria parasiteEMBO reports · 2019Article
- Histone 4 lysine 8 acetylation regulates proliferation and host-pathogen interaction in Plasmodium falciparum.Epigenetics & chromatin · 2017Article
- Quantitative chromatin proteomics reveals a dynamic histone post-translational modification landscape that defines asexual and sexual Plasmodium falciparum parasites.Scientific reports · 2017Article
- Dynamic and Combinatorial Landscape of Histone Modifications during the Intraerythrocytic Developmental Cycle of the Malaria Parasite.Journal of proteome research · 2016Article
- Characterization of an A-kinase anchoring protein-like suggests an alternative way of PKA anchoring in Plasmodium falciparum.Malaria journal · 2016Article
- Analysis of the interactome of the Ser/Thr Protein Phosphatase type 1 in Plasmodium falciparum.BMC genomics · 2016Article
- Plasmodium falciparum PfSET7: enzymatic characterization and cellular localization of a novel protein methyltransferase in sporozoite, liver and erythrocytic stage parasites.Scientific reports · 2016Article
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
The important role of histone posttranslational modifications, particularly methylation and acetylation, in Plasmodium falciparum gene regulation has been established. However, the role of histone phosphorylation remains understudied. Here, we investigate histone phosphorylation utilizing liquid chromatography and tandem mass spectrometry to analyze histones extracted from asexual blood stages using two improved protocols to enhance preservation of PTMs. Enrichment for phosphopeptides lead to the detection of 14 histone phospho-modifications in P. falciparum. The majority of phosphorylation sites were observed at the N-terminal regions of various histones and were frequently observed adjacent to acetylated lysines. We also report the identification of one novel member of the P. falciparum histone phosphosite binding protein repertoire, Pf14-3-3I. Recombinant Pf14-3-3I protein bound to purified parasite histones. In silico structural analysis of Pf14-3-3 proteins revealed that residues responsible for binding to histone H3 S10ph and/or S28ph are conserved at the primary and the tertiary structure levels. Using a battery of H3 specific phosphopeptides, we demonstrate that Pf14-3-3I preferentially binds to H3S28ph over H3S10ph, independent of modification of neighbouring residues like H3S10phK14ac and H3S28phS32ph. Our data provide key insight into histone phosphorylation sites. The identification of a second member of the histone modification reading machinery suggests a widespread use of histone phosphorylation in the control of various nuclear processes in malaria parasites.
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