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Kirchhoff, H., Institute of Biological Chemistry, Washington State University, Pullman, WA 99164, United States
Hall, C., Institute of Biological Chemistry, Washington State University, Pullman, WA 99164, United States
Wood, M., Institute of Biological Chemistry, Washington State University, Pullman, WA 99164, United States
Herbstov√°, M., Institute of Biological Chemistry, Washington State University, Pullman, WA 99164, United States
Tsabari, O., Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel
Nevo, R., Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel
Charuvi, D., Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel
Shimoni, E., Electron Microscopy Unit, Weizmann Institute of Science, Rehovot 76100, Israel
Reich, Z., Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel
The machinery that conducts the light-driven reactions of oxygenic photosynthesis is hosted within specialized paired membranes called thylakoids. In higher plants, the thylakoids are segregated into two morphological and functional domains called grana and stroma lamellae. A large fraction of the luminal volume of the granal thylakoids is occupied by the oxygen-evolving complex of photosystem II. Electron microscopy data we obtained on dark- and light-adapted Arabidopsis thylakoids indicate that the granal thylakoid lumen significantly expands in the light. Models generated for the organization of the oxygen-evolving complex within the granal lumen predict that the light-induced expansion greatly alleviates restrictions imposed on protein diffusion in this compartment in the dark. Experiments monitoring the redox kinetics of the luminal electron carrier plastocyanin support this prediction. The impact of the increase in protein mobility within the granal luminal compartment in the light on photosynthetic electron transport rates and processes associated with the repair of photodamaged photosystem II complexes is discussed.
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Dynamic control of protein diffusion within the granal thylakoid lumen
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Kirchhoff, H., Institute of Biological Chemistry, Washington State University, Pullman, WA 99164, United States
Hall, C., Institute of Biological Chemistry, Washington State University, Pullman, WA 99164, United States
Wood, M., Institute of Biological Chemistry, Washington State University, Pullman, WA 99164, United States
Herbstov√°, M., Institute of Biological Chemistry, Washington State University, Pullman, WA 99164, United States
Tsabari, O., Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel
Nevo, R., Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel
Charuvi, D., Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel
Shimoni, E., Electron Microscopy Unit, Weizmann Institute of Science, Rehovot 76100, Israel
Reich, Z., Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel
Dynamic control of protein diffusion within the granal thylakoid lumen
The machinery that conducts the light-driven reactions of oxygenic photosynthesis is hosted within specialized paired membranes called thylakoids. In higher plants, the thylakoids are segregated into two morphological and functional domains called grana and stroma lamellae. A large fraction of the luminal volume of the granal thylakoids is occupied by the oxygen-evolving complex of photosystem II. Electron microscopy data we obtained on dark- and light-adapted Arabidopsis thylakoids indicate that the granal thylakoid lumen significantly expands in the light. Models generated for the organization of the oxygen-evolving complex within the granal lumen predict that the light-induced expansion greatly alleviates restrictions imposed on protein diffusion in this compartment in the dark. Experiments monitoring the redox kinetics of the luminal electron carrier plastocyanin support this prediction. The impact of the increase in protein mobility within the granal luminal compartment in the light on photosynthetic electron transport rates and processes associated with the repair of photodamaged photosystem II complexes is discussed.
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