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• W1968915087 endingPage "117" @default.
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• W1968915087 abstract "The effective antenna size of Photosystem II is regulated by a kinase mediated phosphorylation of the main light-harvesting chlorophyll ab protein (LHCII). This regulatory mechanism, which involves lateral migration of the phospho-protein along the thylakoid membrane, is thought to be essential for short term acclimation of the photosynthetic light harvesting. In this study we have analyzed how LHCII phosphorylation and the subsequent changes in the organization of the thylakoid membrane are influenced by low temperatures. It was shown that the kinase activity, measured as degree of LHCII phosphorylation, is operational at 0°C although partially inhibited. By subfractionation of thylakoid membranes phosphorylated at 0°C it was shown that virtually no phospho-LHCII migrates to the stroma thylakoids at this low temperature, in contrast to the case at normal temperatures. When such thylakoids, with phospho-LHCII retained in the appressed grana regions, were gradually subjected to increasing temperatures followed by subfractionation, it was shown that rapid lateral migration of phospho-LHCII was induced in a quite narrow temperature range of 10–12°C. At 5°C the migration of phospho LHCII would require hours for completion while at 20°C all phospho-LHCII had arrived in the stroma thylakoids within 5 min. From a functional point of view, our results reveal that at temperatures when the migration of phospho-LHCII from the grana region is prevented, there is no reduction in the effective antenna size of Photosystem II. This shows that protein phosphorylation in itself is not sufficient to create a functional disconnection between Photosystem II and LHCII but that the subsequent lateral diffusion of phospho-LHCII in the thylakoid membrane is required. The significance of the results in connection with increased photoinhibition during combined light and cold stress is discussed. Apart from these physiological implications, the present combination of protein phosphorylation and thylakoid subfractionation offers a novel way to study lateral diffusion of a single protein in an undisturbed biomembrane." @default.
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• W1968915087 date "1992-02-01" @default.
• W1968915087 modified "2023-09-25" @default.
• W1968915087 title "Low temperature effects on thylakoid protein phosphorylation and membrane dynamics" @default.
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• W1968915087 doi "https://doi.org/10.1016/0005-2728(92)90206-h" @default.
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