Research interests of the group are focused on various aspects of ribosomal protein synthesis, in particular the biogenesis of integral membrane proteins in bacteria.
In one project we are examining the function of the signal recognition particle (SRP) in the biosynthesis of membrane proteins. SRP binds to ribosomes translating membrane proteins, recognizing a hydrophobic signal sequence that is part of the nascent peptide. By an interaction with the SRP receptor those ribosomes are targeted to the translocation pore ("translocon") in the membrane, forming a quaternary transfer complex. We are interested in the dynamics of that complex, including the dynamics of the translocon, that allows membrane proteins to insert into the membrane in a co-translational fashion.
In a related project we are studying the interplay between various ribosome-associated protein biogenesis factors, including SRP, the chaperone trigger factor as well as the modifying enzymes peptide deformylase and methionine aminopeptidase. We use methods of biochemistry and molecular biology, as well as biophysical techniques, such as fluorescence, including single-molecule fluorescence, rapid kinetics (stopped flow, quench flow), and others.