Abstract
Covalent modifications of the N‐termini of core histone proteins are essential to gene transcription. One such modification is the monoubiquitylation of histone H2B, which has been shown in all eukaryotes tested so far. However, this process has not been examined in Giardia lamblia, a primitive eukaryotic parasite of the intestinal tract. Two techniques are being pursued to test for the monoubiquitylation of histone H2B: western blotting and liquid chromatography/mass spectroscopy (LC/MS). Discovering whether monoubiquitylated histone H2B occurs in G. lamblia will help to show when mechanisms of chromatin modifications arose in eukaryotes as well as provide important biological information about a dangerous parasite.
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