This study followed a previous report in which a histone acetyltransferase was found to be responsible for acetylation of H3K9 at putative transcriptional initiation sites and implicated in transcriptional regulation of Plasmodium genes. Extensive studies of epigenetic silencing of subtelomericaly located variable surface antigen families, namely the var gene family, have also been carried out. Here it was shown that epigenetic markers represented by specific histone modifications including both acetylation and methylation, were associated with the mutually exclusive expression of individual var genes. Lopez-Rubio demonstrated that the var gene silencing is mediated by tri-methylation of histone 3 at lysine residue 9 which concentrates in distinct compartments at the nuclear periphery. In addition, at least additional three distinct Zatebradine pattern of nuclear distribution were found for other types of histone modifications. A continuous ����horseshoe-like���� pattern around the nuclear Iberdomide periphery was observed for H3K4Me3, and H4K20Me3, typically markers of gene activation and repression, respectively. In contrast, H3K4Me2 another activation marker showed a strong punctuate distribution spread throughout the nuclei. The most striking pattern was observed for H3K79Me3 that was characterized by 3-5 distinct dots clustered at a one end on the nuclei. Taken together, these data suggested that the localization may be a major prerequisite for specific biological roles of the histone isoforms in gene expression, marking distinct regions of chromatin distribution in the nuclei. Besides the role of the H3K9Me3 in the silencing of the subtelomeric gene families that has been linked with the two perinuclear foci, close to nothing is known about the biological significance of the different subnuclear compartments. Here we aim to characterize intracellular distributions of several previously uncharacterized histone modifications including four types of acetylations H4K5Ac, H4K8Ac, H3K9Ac and H4K5,8,12,16 tetraAc and one methylation H3K9Me1. The protein distribution pattern of the studied histone acetylations resembles the horseshoe-like pattern observed for H3K4Me3 suggesting their overlapping roles in gene expression.