[SCAN] Visualizing bacterial protein interactions by FLIM-FRET

A powerful approach to study transient protein interactions, in vivo, at subcellular resolution is Fluorescence Lifetime Imaging Microscopy-Förster Resonance Energy Transfer (FLIM-FRET). FLIM-FRET allows probing protein complex dynamics and provides information on when and where their interactions take place. However, due to its technical complexity, it has not been routinely applied to study protein interactions in bacterial cells.

At the SCAN, I will discuss our efforts to set up FLIM-FRET as a robust technique for bacteria. Control interactions in single living S. aureus cells will be demonstrated and fluorescence lifetime localization patterns of several cell division and cell wall synthesis proteins will be presented.