Regulatory proteolysis of the major light-harvesting chlorophyll a/b protein of photosystem II by a light-induced membrane-associated enzymic system.

An endogenous proteolytic activity associated with spinach chloroplast thylakoid membranes has been identified. This enzymic activity is involved in the degradation of the major light-harvesting chlorophyll a/b protein of photosystem II (LHCII) in response to exposure of leaves to increased irradiance. This proteolysis of LHCII requires an induction period and can only be detected 48-72 hours after transfer of the plants from low-intensity to high-intensity light. Once initiated by high-intensity light, the degradation of LHCII can readily occur in complete darkness. The proteolysis can, after induction in vivo, be experimentally followed in vitro, both in isolated intact chloroplasts and thylakoid membranes. The proteolytic process is strictly dependent on ATP and the protease involved is of the serine or cysteine type. The activity can be released from isolated thylakoid membranes by washing with high concentrations of NaCl and reconstituted by readdition of the desalted wash supernatant. It is concluded that the protease is extrinsically bound to the outer surface of the stroma-exposed regions of the stacked thylakoid membrane. The mechanism for the induction of the proteolytic process as well as its relation to previously described thylakoid proteases will be discussed.