Using a Forster Resonance Energy Transfer-Based Method to Identify a Protein, YcgR, that is Able to Bind c-di-GMP Molecules in Living Bacterial Cells
Mentor 1
Ching-Hong Yang
Location
Union Wisconsin Room
Start Date
29-4-2016 1:30 PM
End Date
29-4-2016 3:30 PM
Description
C-di-GMP acts as a global regulatory signal used by many bacteria to regulate diverse cellular activities such as motility, biofilm formation, and virulence. The c-di-GMP levels of bacterial cells is controlled by diguanylate cyclase (DGC) and c-di-GMP phosphodiesterases (PDE). DGC synthesizes c-di-GMP from two molecules of GTP. PDE is able to degrade c-di-GMP by breaking it down into pGpG. C-di-GMP relies on cellular c-di-GMP effector proteins in order to exert diverse influences in the cell. These effector proteins act by sensing the intracellular levels of c-di-GMP and directly bind with c-di-GMP. Using a Forster resonance energy transfer (FRET)-based method, we identified a protein, YcgR, that is an effector protein and is able to bind c-di-GMP in living bacterial cells.
Using a Forster Resonance Energy Transfer-Based Method to Identify a Protein, YcgR, that is Able to Bind c-di-GMP Molecules in Living Bacterial Cells
Union Wisconsin Room
C-di-GMP acts as a global regulatory signal used by many bacteria to regulate diverse cellular activities such as motility, biofilm formation, and virulence. The c-di-GMP levels of bacterial cells is controlled by diguanylate cyclase (DGC) and c-di-GMP phosphodiesterases (PDE). DGC synthesizes c-di-GMP from two molecules of GTP. PDE is able to degrade c-di-GMP by breaking it down into pGpG. C-di-GMP relies on cellular c-di-GMP effector proteins in order to exert diverse influences in the cell. These effector proteins act by sensing the intracellular levels of c-di-GMP and directly bind with c-di-GMP. Using a Forster resonance energy transfer (FRET)-based method, we identified a protein, YcgR, that is an effector protein and is able to bind c-di-GMP in living bacterial cells.
