A unique study by scientists from the IEM CAS and the BIOCEV research centre shows new properties of the SMARCA5 protein

The PLOS ONE journal (open in a new window)(IF 2.9) has published a new co-authored study on identifying and characterising novel properties of the chromatin remodelling protein SMARCA5. The authors of the study are Pavel Čabart from the Department of Cell Nucleus Plasticity of the IEM CAS and Prokopis C. Andrikopoulos from the BIOCEV research centre.

The development of very efficient protein separation and analysis techniques has determined the massive development in protein chemistry in the last fifty years. Most of these techniques exploit different properties of molecules, such as their mass or charge. In the last twenty years, however, a group of experimental and computational methods based on specific interactions between biomolecules and ligands has gained importance. Among the theoretical and computational approaches, quantum mechanics has a prominent position.

The authors of the study provided evidence that the SMARCA5 protein forms chelate bonds with divalent transition metal cations (cobalt, copper, zinc and nickel) on a solid support. They exploited this property to isolate the protein using immobilized metal affinity chromatography (IMAC). They investigated the types of bonds using IMAC and quantum mechanics calculations. The results of the study may be inspiring for investigating possible functional interactions between transition metals and the SMARCA5 protein in the cell. Specifically, modulation of its nucleosome-translocation activity and conformational changes, which in turn stabilise its interaction with accessory subunits within chromatin remodelling complexes or with antiviral immunity-enhancing proteins.