Eukaryotic cells require the precisely timed activation of genes, which corresponds with chromatin alterations. Examples of such modification are addition of the protein ubiquitin, a process referred to as ubiquitination. Abnormal levels of ubiquitin action in histone H2B are found in various diseases, including cancer. Despite this, the ubiquitination process across genic nucleosomes remains unclear. In a new paper published in Nature, researchers suggest liquid phase separation as the underlying mechanism of H2B ubiquitination. The researchers used TRITC-dextran 40 from TdB for the ubiquitination assay experiments. Read the full article here.
