Evidence map›Paper›PMID 25713340›Full record

ArticlePlant physiology2015

Photoprotection conferred by changes in photosynthetic protein levels and organization during dehydration of a homoiochlorophyllous resurrection plant.

Dana Charuvi, Reinat Nevo, Eyal Shimoni, Leah Naveh, Ahmad Zia, Zach Adam, Jill M Farrant, Helmut Kirchhoff, Ziv Reich

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.6field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed, 55 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Acclimation of the Resurrection PlantPlants (Basel, Switzerland) · 2024
    Article
  7. Article
  8. Review
  9. Diversification of Plastid Structure and Function in Land Plants.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Fundamental helical geometry consolidates the plant photosynthetic membrane.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 5 institutions in 3 countries.

Dana CharuviDepartment of Biological Chemistry (D.C., R.N., Z.R.) and Electron Microscopy Unit (E.S.), Weizmann Institute of Science, Rehovot 76100, Israel;Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, Hebrew University of Jerusalem, Rehovot 76100, Israel (L.N., Z.A.);Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340 (A.Z., H.K.); andDepartment of Molecular and Cell Biology, University of Cape Town, Rondebosch 7701, South Africa (J.M.F.).
Reinat NevoDepartment of Biological Chemistry (D.C., R.N., Z.R.) and Electron Microscopy Unit (E.S.), Weizmann Institute of Science, Rehovot 76100, Israel;Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, Hebrew University of Jerusalem, Rehovot 76100, Israel (L.N., Z.A.);Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340 (A.Z., H.K.); andDepartment of Molecular and Cell Biology, University of Cape Town, Rondebosch 7701, South Africa (J.M.F.).
Eyal ShimoniDepartment of Biological Chemistry (D.C., R.N., Z.R.) and Electron Microscopy Unit (E.S.), Weizmann Institute of Science, Rehovot 76100, Israel;Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, Hebrew University of Jerusalem, Rehovot 76100, Israel (L.N., Z.A.);Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340 (A.Z., H.K.); andDepartment of Molecular and Cell Biology, University of Cape Town, Rondebosch 7701, South Africa (J.M.F.).
Leah NavehDepartment of Biological Chemistry (D.C., R.N., Z.R.) and Electron Microscopy Unit (E.S.), Weizmann Institute of Science, Rehovot 76100, Israel;Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, Hebrew University of Jerusalem, Rehovot 76100, Israel (L.N., Z.A.);Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340 (A.Z., H.K.); andDepartment of Molecular and Cell Biology, University of Cape Town, Rondebosch 7701, South Africa (J.M.F.).
Ahmad ZiaDepartment of Biological Chemistry (D.C., R.N., Z.R.) and Electron Microscopy Unit (E.S.), Weizmann Institute of Science, Rehovot 76100, Israel;Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, Hebrew University of Jerusalem, Rehovot 76100, Israel (L.N., Z.A.);Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340 (A.Z., H.K.); andDepartment of Molecular and Cell Biology, University of Cape Town, Rondebosch 7701, South Africa (J.M.F.).
Zach AdamDepartment of Biological Chemistry (D.C., R.N., Z.R.) and Electron Microscopy Unit (E.S.), Weizmann Institute of Science, Rehovot 76100, Israel;Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, Hebrew University of Jerusalem, Rehovot 76100, Israel (L.N., Z.A.);Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340 (A.Z., H.K.); andDepartment of Molecular and Cell Biology, University of Cape Town, Rondebosch 7701, South Africa (J.M.F.).
Jill M FarrantDepartment of Biological Chemistry (D.C., R.N., Z.R.) and Electron Microscopy Unit (E.S.), Weizmann Institute of Science, Rehovot 76100, Israel;Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, Hebrew University of Jerusalem, Rehovot 76100, Israel (L.N., Z.A.);Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340 (A.Z., H.K.); andDepartment of Molecular and Cell Biology, University of Cape Town, Rondebosch 7701, South Africa (J.M.F.).
Helmut KirchhoffDepartment of Biological Chemistry (D.C., R.N., Z.R.) and Electron Microscopy Unit (E.S.), Weizmann Institute of Science, Rehovot 76100, Israel;Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, Hebrew University of Jerusalem, Rehovot 76100, Israel (L.N., Z.A.);Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340 (A.Z., H.K.); andDepartment of Molecular and Cell Biology, University of Cape Town, Rondebosch 7701, South Africa (J.M.F.).
Ziv ReichDepartment of Biological Chemistry (D.C., R.N., Z.R.) and Electron Microscopy Unit (E.S.), Weizmann Institute of Science, Rehovot 76100, Israel;Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, Hebrew University of Jerusalem, Rehovot 76100, Israel (L.N., Z.A.);Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340 (A.Z., H.K.); andDepartment of Molecular and Cell Biology, University of Cape Town, Rondebosch 7701, South Africa (J.M.F.) ziv.reich@weizmann.ac.il.
Hebrew University of Jerusalem · ILUnited States Nuclear Regulatory Commission · USWashington State University · USWeizmann Institute of Science · ILUniversity of Cape Town · ZA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

CraterostigmaCytochrome b6f ComplexDehydrationDesiccationElectron TransportLightPhotosynthesisPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexPlant LeavesPlant ProteinsWaterCytochrome b6f ComplexPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexPlant ProteinsWater

Identifiers

PMID25713340
PMCPMC4378169
OpenAlexW2089159924

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