Regulation of thylakoid protein phosphorylation by the thiol redox state - the role of thioredoxin

摘要

A number of thylakoid proteins belonging to photosystem II (PSII) are phosphorylated in a light dependent manner. Among these are the reaction center proteins of PSII, D1 and D2, as well as the major chlorophyll a/b light-harvesting antenna (LHCII) (Allen, 1992). Thylakoid protein phosphorylation is believed to play an important role in the regulation of light energy distribution (state transitions), in long-term acclimation of the antenna size and in the control of D1 protein turnover (Allen 1992;Andersson and Aro 1997). Light activation of protein phosphorylation involves the reduction of plastoquinone (Allen, 1992) and, at least in the case of phosphorylation of LHCII, binding of plastoquinol at the quinol oxidising site in cytochrome bf (Veneret al. 1998).