Fluorescence based single-molecule studies of bacterial protein synthesis, in vitro and in vivo
The main focus of our research is to study protein synthesis dynamics at high spatial and temporal resolution inside living cells, with the aim of connecting molecular interactions with cell physiology and population biology.
Ribosome catalyzed protein synthesis is one of the most fundamental processes in all life forms. From decades of research, the combination of traditional biochemistry; structural approaches including NMR, cryo-EM, x-ray crystallography; and more recently single-molecule fluorescence based in vitro techniques probing structure and dynamics at the same time, have led to a very detailed picture of the molecular mechanisms of ribosome catalyzed protein synthesis. However, we have very sparse information about the dynamics of protein synthesis, in particular inside living cells, one major problem being the vast number of ribosomes in the cell pursuing different tasks at any given moment. The sheer complexity of the translational system (do we know all the players yet?), and its interplay with other processes, make it very hard to connect the molecular details of protein synthesis with cell physiology and population biology. Our research aims at connecting all these dots, in space and time, to get a coherent picture of one of the most fundamental processes of life. This is done by studying key components of the protein machinery, one by one, performing their daily work inside the living cell.
In vivo experiments are complimented by traditional biochemistry as well as in vitro single molecule fluorescence microscopy methods.
Single-molecule fluorescence microscopy, single particle tracking, super-resolution microscopy, Total Internal Reflection Fluorescence (TIRF) microscopy, ensemble biochemical methods etc.