抄録
The turnover of Photosystem II (PSII) has been shortly described as stress-induced damage of the D1 protein followed by monomerization of the PSII complex and its movement to the stroma lamella. The De-phosphorylation of the D1 protein triggers the activation of proteases to start its degradation and subsequent incorporation and synthesis of a new copy of the D1 protein into the PSII monomer.
Here we described a more refined view of the turnover of PSII, the de-phosphorylation of PSII core proteins triggers the swelling of thylakoid grana stacks and the binding of hexameric FtsH proteases to the PSII supercomplexes. Upon de-phosphorylation of CP43, it gets separated from the PSII monomer and makes a room for the hexameric FtsH to start degrading the damaged D1 protein. After degradaton of the D1 protein the FtsH becomes unstable and is fast deactivated.
