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Photoprotection conferred by changes in photosynthetic protein levels and organization during dehydration of a homoiochlorophyllous resurrection plant
Year:
2015
Authors :
חרובי, דנה
;
.
Volume :
167
Co-Authors:
Charuvi, D., Department of Biological Chemistry, Weizmann Institute of Science, Rehovot, Israel
Nevo, R., Department of Biological Chemistry, Weizmann Institute of Science, Rehovot, Israel
Shimoni, E., Electron Microscopy Unit, Weizmann Institute of Science, Rehovot, Israel
Naveh, L., Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, Hebrew University of Jerusalem, Rehovot, Israel
Zia, A., Institute of Biological Chemistry, Washington State University, Pullman, WA, United States, Crop Physiology and Breeding, Commonwealth Scientific and Industrial Research Organization Plant Industry, GPO Box 1600, Canberra, ACT, South Africa
Adam, Z., Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, Hebrew University of Jerusalem, Rehovot, Israel
Farrant, J.M., Department of Molecular and Cell Biology, University of Cape Town, Rondebosch, South Africa
Kirchhoff, H., Institute of Biological Chemistry, Washington State University, Pullman, WA, United States
Reich, Z., Department of Biological Chemistry, Weizmann Institute of Science, Rehovot, Israel
Facilitators :
From page:
1554
To page:
1565
(
Total pages:
12
)
Abstract:
During desiccation, homoiochlorophyllous resurrection plants retain most of their photosynthetic apparatus, allowing them to resume photosynthetic activity quickly upon water availability. These plants rely on various mechanisms to prevent the formation of reactive oxygen species and/or protect their tissues from the damage they inflict. In this work, we addressed the issue of how homoiochlorophyllous resurrection plants deal with the problem of excessive excitation/electron pressures during dehydration using Craterostigma pumilum as a model plant. To investigate the alterations in the supramolecular organization of photosynthetic protein complexes, we examined cryoimmobilized, freeze-fractured leaf tissues using (cryo)scanning electron microscopy. These examinations revealed rearrangements of photosystem II (PSII) complexes, including a lowered density during moderate dehydration, consistent with a lower level of PSII proteins, as shown by biochemical analyses. The latter also showed a considerable decrease in the level of cytochrome f early during dehydration, suggesting that initial regulation of the inhibition of electron transport is achieved via the cytochrome b6f complex. Upon further dehydration, PSII complexes are observed to arrange into rows and semicrystalline arrays, which correlates with the significant accumulation of sucrose and the appearance of inverted hexagonal lipid phases within the membranes. As opposed to PSII and cytochrome f, the light-harvesting antenna complexes of PSII remain stable throughout the course of dehydration. Altogether, these results, along with photosynthetic activity measurements, suggest that the protection of retained photosynthetic components is achieved, at least in part, via the structural rearrangements of PSII and (likely) light-harvesting antenna complexes into a photochemically quenched state. © 2015 American Society of Plant Biologists.All Rights Reserved.
Note:
Related Files :
Craterostigma pumilum
Selaginella pilifera
עוד תגיות
תוכן קשור
More details
DOI :
10.1104/pp.114.255794
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
30361
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:53
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Scientific Publication
Photoprotection conferred by changes in photosynthetic protein levels and organization during dehydration of a homoiochlorophyllous resurrection plant
167
Charuvi, D., Department of Biological Chemistry, Weizmann Institute of Science, Rehovot, Israel
Nevo, R., Department of Biological Chemistry, Weizmann Institute of Science, Rehovot, Israel
Shimoni, E., Electron Microscopy Unit, Weizmann Institute of Science, Rehovot, Israel
Naveh, L., Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, Hebrew University of Jerusalem, Rehovot, Israel
Zia, A., Institute of Biological Chemistry, Washington State University, Pullman, WA, United States, Crop Physiology and Breeding, Commonwealth Scientific and Industrial Research Organization Plant Industry, GPO Box 1600, Canberra, ACT, South Africa
Adam, Z., Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, Hebrew University of Jerusalem, Rehovot, Israel
Farrant, J.M., Department of Molecular and Cell Biology, University of Cape Town, Rondebosch, South Africa
Kirchhoff, H., Institute of Biological Chemistry, Washington State University, Pullman, WA, United States
Reich, Z., Department of Biological Chemistry, Weizmann Institute of Science, Rehovot, Israel
Photoprotection conferred by changes in photosynthetic protein levels and organization during dehydration of a homoiochlorophyllous resurrection plant
During desiccation, homoiochlorophyllous resurrection plants retain most of their photosynthetic apparatus, allowing them to resume photosynthetic activity quickly upon water availability. These plants rely on various mechanisms to prevent the formation of reactive oxygen species and/or protect their tissues from the damage they inflict. In this work, we addressed the issue of how homoiochlorophyllous resurrection plants deal with the problem of excessive excitation/electron pressures during dehydration using Craterostigma pumilum as a model plant. To investigate the alterations in the supramolecular organization of photosynthetic protein complexes, we examined cryoimmobilized, freeze-fractured leaf tissues using (cryo)scanning electron microscopy. These examinations revealed rearrangements of photosystem II (PSII) complexes, including a lowered density during moderate dehydration, consistent with a lower level of PSII proteins, as shown by biochemical analyses. The latter also showed a considerable decrease in the level of cytochrome f early during dehydration, suggesting that initial regulation of the inhibition of electron transport is achieved via the cytochrome b6f complex. Upon further dehydration, PSII complexes are observed to arrange into rows and semicrystalline arrays, which correlates with the significant accumulation of sucrose and the appearance of inverted hexagonal lipid phases within the membranes. As opposed to PSII and cytochrome f, the light-harvesting antenna complexes of PSII remain stable throughout the course of dehydration. Altogether, these results, along with photosynthetic activity measurements, suggest that the protection of retained photosynthetic components is achieved, at least in part, via the structural rearrangements of PSII and (likely) light-harvesting antenna complexes into a photochemically quenched state. © 2015 American Society of Plant Biologists.All Rights Reserved.
Scientific Publication
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