Dynamic association of the H3K64 trimethylation mark with genes encodingexported proteins in Plasmodium falciparum.
Jabeena, C A et al.
Epigenetic modifications have emerged as critical regulators of virulence genes and stage-specific gene expression in Plasmodium falciparum. However, the specific roles of histone core epigenetic modifications in regulating the stage-specific gene expression are not well understood. In this study, we report an unconventional trimethylation at lysine 64 on histone 3 (H3K64me3) and characterize its functional relevance in P. falciparum. We show that PfSET4 and PfSET5 proteins of P. falciparum methylate H3K64 and that they prefer the nucleosome as a substrate over free histone 3 proteins. Structural analysis of PfSET5 revealed that it interacts with the nucleosome as a dimer. The H3K64me3 mark is dynamic, being enriched in the ring and trophozoite stages and drastically reduced in schizont stages. Stage-specific global ChIP-sequencing analysis of the H3K64me3 mark revealed the selective enrichment of this methyl mark on the genes of exported family proteins in the ring and trophozoite stages, and a significant reduction of the same in the schizont stages. Collectively, our data identify a novel epigenetic mark that are associated with the subset of genes encoding for exported proteins which may regulate their expression in different stages of P. falciparum.
To ensure you see the information most relevant to you, please select your country.
Please note that your browser will need to be configured to accept cookies.
Diagenode will process your personal data in strict accordance with its privacy policy. This will include sending you updates about us, our products, and resources we think would be of interest to you.
