The main thylakoid membrane lipid monogalactosyldiacylglycerol (MGDG) promotes the de-epoxidation of violaxanthin associated with the light-harvesting complex of photosystem II (LHCII)

• Published in: Biochimica et biophysica acta 2010-03, Vol.1797 (3), p.414-424
• Main Authors: Schaller, Susann, Latowski, Dariusz, Jemioła-Rzemińska, Małgorzata, Wilhelm, Christian, Strzałka, Kazimierz, Goss, Reimund
• Format: Article
• Language: English
• Subjects: Bilayer lipid; Binding Sites; Galactolipids - pharmacology; Inverted hexagonal phase; Light-harvesting complex; Light-Harvesting Protein Complexes - metabolism; Lipid Bilayers; MGDG; Non-bilayer lipid; Oxidoreductases - metabolism; Photosystem II Protein Complex - metabolism; Spinacia oleracea - chemistry; Thylakoid membrane; Thylakoids - metabolism; Xanthophyll cycle; Xanthophylls - chemistry
• ISSN: 0005-2728; 0006-3002; 1879-2650
• DOI: 10.1016/j.bbabio.2009.12.011

In higher plants, the major part of the xanthophyll cycle pigment violaxanthin (Vx) is non-covalently bound to the main light-harvesting complex of PSII (LHCII). Under saturating light conditions Vx has to be released from its binding site into the surrounding lipid phase, where it is converted to zeaxanthin (Zx) by the enzyme Vx de-epoxidase (VDE). In the present study we investigated the influence of thylakoid lipids on the de-epoxidation of Vx, which was still associated with the LHCII. We isolated LHCII with different concentrations of native, endogenous lipids and Vx by sucrose gradient centrifugation or successive cation precipitation. Analysis of the different LHCII preparations showed that the concentration of LHCII-associated Vx was correlated with the concentration of the main thylakoid lipid monogalactosyldiacylglycerol (MGDG) associated with the complexes. Decreases in the MGDG content of the LHCII led to a diminished Vx concentration, indicating that a part of the total Vx pool was located in an MGDG phase surrounding the LHCII, whereas another part was bound to the LHCII apoproteins. We further studied the convertibility of LHCII-associated Vx in in-vitro enzyme assays by addition of isolated VDE. We observed an efficient and almost complete Vx conversion in the LHCII fractions containing high amounts of endogenous MGDG. LHCII preparations with low concentrations of MGDG exhibited a strongly reduced Vx de-epoxidation, which could be increased by addition of exogenous, pure MGDG. The de-epoxidation of LHCII-associated Vx was saturated at a much lower concentration of native, endogenous MGDG compared with the concentration of isolated, exogenous MGDG, which is needed for optimal VDE activity in in-vitro assays employing pure isolated Vx.