Bas Pieters

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Lab 6.15


In eukaryotic cells DNA is coiled around histone protein complexes called nucleosomes. These histones are susceptible to modifications by various machineries, leading to phosphorylation, acetylation, methylation and other types of post-translational modifications (PTMs), which play crucial roles in the regulation of gene expression. An example is the trimethylation of lysine 4 of histone 3 (H3K4me3), which is particularly found in euchromatin. During the past decade, the field of epigenetics has advanced strongly and many writers, readers and erasers of the histone code have been identified and characterized.

(Combinations of) modified amino acids on histones can be specifically recognized by specialized proteins, provided  the nucleosomes are accessible for such proteins. This has led to the histone code hypothesis, postulating that these PTMs are involved in gene regulation. Increasing evidence confirms this and demonstrates that various types of cancer, such as leukemia, are associated with deregulation of these processes.

As a PhD candidate working in the field of epigenetics, together with Dr. Jasmin Mesinovic, I am currently investigating the interactions between H3K4me3 and the aromatic cage found in various H3K4me3 reader proteins.  To facilitate this work in the overlapping fields of biochemistry and chemistry, I am performing part of my research in the laboratory of Biomolecular Chemistry and another part in the Organic Chemistry laboratory.

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