Evidence map›Paper›PMID 8265658›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1993

Two functionally distinct forms of the photosystem II reaction-center protein D1 in the cyanobacterium Synechococcus sp. PCC 7942.

A K Clarke, V M Hurry, P Gustafsson, G Oquist

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

30 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. Comparative Thermophysiology of MarineFrontiers in microbiology · 2022
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Cyanobacterial psbA gene family: optimization of oxygenic photosynthesis.Cellular and molecular life sciences : CMLS · 2009
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Chlorophyll fluorescence analysis of cyanobacterial photosynthesis and acclimation.Microbiology and molecular biology reviews : MMBR · 1998
    Review
  17. Article
  18. The cyanobacterium Synechococcus resists UV-B by exchanging photosystem II reaction-center D1 proteins.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  19. 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

4 authors at 1 institution in 1 country.

A K ClarkeDepartment of Plant Physiology, University of Umeå, Sweden.
V M Hurry
P Gustafsson
G Oquist
Umeå University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cyanobacterium Synechococcus sp. PCC 7942 possesses a small psbA multigene family that codes for two distinct forms of the photosystem II reaction-center protein D1 (D1:1 and D1:2). We showed previously that the normally predominant D1 form (D1:1) was rapidly replaced with the alternative D1:2 when cells adapted to a photon irradiance of 50 mumol.m-2.s-1 are shifted to 500 mumol.m-2.s-1 and that this interchange was readily reversible once cells were allowed to recover under the original growth conditions. By using the psbA inactivation mutants R2S2C3 and R2K1 (which synthesize only D1:1 and D1:2, respectively), we showed that this interchange between D1 forms was essential for limiting the degree of photoinhibition as well as enabling a rapid recovery of photosynthesis. In this report, we have extended these findings by examining whether any intrinsic functional differences exist between the two D1 forms that may afford increased resistance to photoinhibition. Initial studies on the rate of D1 degradation at three photon irradiances (50, 200, and 500 mumol.m-2.s-1) showed that the rates of degradation for both D1 forms increase with increasing photon flux density but that there was no significant difference between D1:1 and D1:2. Analysis of light-response curves for oxygen evolution for the mutants R2S2C3 and R2K1 revealed that cells with photosystem II reaction centers containing D1:2 have a higher apparent quantum yield (approximately 25%) than cells possessing D1:1. Further studies using chlorophyll a fluorescence measurements confirmed that R2K1 has a higher photochemical yield than R2S2C3; that is, a more efficient conversion of excitation energy from photon absorption into photochemistry. We believe that the higher photochemical efficiency of reaction centers containing D1:2 is causally related to the preferential induction of D1:2 at high light and thus may be an integral component of the protection mechanism within Synechococcus sp. PCC 7942 against photoinhibition.

Indexed as

Bacterial ProteinsChlorophyllChlorophyll ACyanobacteriaGenes, BacterialKineticsLightMultigene FamilyMutagenesisPhotosynthesisPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexPlant ProteinsBacterial ProteinsChlorophyllChlorophyll APhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexPlant Proteins

Identifiers

PMID8265658
PMCPMC48110
OpenAlexW2000969873

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.