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Phosphorylation of Photosystem II Proteins

  • Chapter
Regulation of Photosynthesis

Part of the book series: Advances in Photosynthesis and Respiration ((AIPH,volume 11))

Summary

Light induces phosphorylation of a number of Photosystem II-related proteins in the thylakoid membrane. Four proteins of Photosystem II (PS II) complex, the D1 and D2 reaction center proteins, the 43-kDa chlorophyll a-binding protein and the psbH gene product are reversibly phosphorylated. Three proteins of the PS II antenna, Lhcb1 and Lhcb2 (designated as LHCII), as well as Lhcb4 also undergo light-dependent phosphorylation. Several studies support the existence of two distinct kinases in the thylakoid membrane, one for phosphorylation of the PS II core proteins and another for the LHCII proteins. Reduction of plastoquinone activates phosphorylation of the PS II core proteins, while both the reduction of a plastoquinone and binding of plastoquinol to the cytochrome b6f complex are required to induce LHCII phosphorylation. Moreover, LHCII phosphorylation is down-regulated under high-light conditions in vivo, and this inactivation is likely to be mediated via the ferredoxin-thioredoxin system in chloroplasts. Both light-dependent and light-independent dephosphorylation of the PS II proteins have been reported. Physiological implications of thylakoid protein phosphorylation include (i) the control of the location and timing of the proteolytic degradation of photodamaged D1 protein by phosphorylation of the PS II core proteins, (ii) the induction of state transitions by reversible LHCII phosphorylation, and (iii) a putative role of the PS II and Lhcb phosphoproteins, or the corresponding kinases and phosphatases, in the relay of signals within chloroplast and from chloroplast to the nucleus to initiate the acclimatization of plants to prevailing environmental conditions.

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Rintamäki, E., Aro, EM. (2001). Phosphorylation of Photosystem II Proteins. In: Aro, EM., Andersson, B. (eds) Regulation of Photosynthesis. Advances in Photosynthesis and Respiration, vol 11. Springer, Dordrecht. https://doi.org/10.1007/0-306-48148-0_23

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