Intrinsically disordered proteins (IDPs) or proteins containing intrinsically disordered regions (IDRs) are ubiquitous in eukaryotic proteome. In contrast to their structurally well-defined counterparts (i.e. folded proteins), IDPs typically lack persistent structure in their native form and do not necessarily require defined structure for molecular recognition and specific function. They are frequently involved in liquid-liquid phase separation (LLPS) driven assembly of various cellular condensates.
We use a large variety of state-of-the-art techniques, ranging from classical biochemical and biophysical tools to in vitro and in-cell single-molecule FRET and live-cell imaging, to understand the mechanisms of IDP interactions and to reveal the basis of specificity for molecular recognition and particular function of IDPs.
The two research axes we are focused in the group are the following:
- investigation of eukaryotic translation initiation and especially the role of disordered translation initiation factors in this process;
- understanding the molecular mechanisms of function of disordered RNA-binding proteins in LLPS and cellular condensates.