Evidence map›Paper›PMID 23011568›Full record

ArticlePlanta2013

Inhibition of chlorophyll biosynthesis at the protochlorophyllide reduction step results in the parallel depletion of Photosystem I and Photosystem II in the cyanobacterium Synechocystis PCC 6803.

Jana Kopečná, Roman Sobotka, Josef Komenda

Abstract read
PubMed Publisher
In one paragraph

Article in Planta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

18 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
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  7. Ycf48 involved in the biogenesis of the oxygen-evolving photosystem II complex is a seven-bladed beta-propeller protein.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  8. Article
  9. Three classes of oxygen-dependent cyclase involved in chlorophyll and bacteriochlorophyll biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
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  16. Review
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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

3 authors at 2 institutions in 1 country.

Jana KopečnáDepartment of Phototrophic Microorganisms, Institute of Microbiology, Academy of Sciences, Opatovický mlýn, Třeboň, Czech Republic.
Roman Sobotka
Josef Komenda
University of South Bohemia in České Budějovice · CZCzech Academy of Sciences, Institute of Microbiology · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In most oxygenic phototrophs, including cyanobacteria, two independent enzymes catalyze the reduction of protochlorophyllide to chlorophyllide, which is the penultimate step in chlorophyll (Chl) biosynthesis. One is light-dependent NADPH:protochlorophyllide oxidoreductase (LPOR) and the second type is dark-operative protochlorophyllide oxidoreductase (DPOR). To clarify the roles of both enzymes, we assessed synthesis and accumulation of Chl-binding proteins in mutants of cyanobacterium Synechocystis PCC 6803 that either completely lack LPOR or possess low levels of the active enzyme due to its ectopic regulatable expression. The LPOR-less mutant grew photoautotrophically in moderate light and contained a maximum of 20 % of the wild-type (WT) Chl level. Both Photosystem II (PSII) and Photosystem I (PSI) were reduced to the same degree. Accumulation of PSII was mostly limited by the synthesis of antennae CP43 and especially CP47 as indicated by the accumulation of reaction center assembly complexes. The phenotype of the LPOR-less mutant was comparable to the strain lacking DPOR that also contained <25 % of the wild-type level of PSII and PSI when cultivated under light-activated heterotrophic growth conditions. However, in the latter case, we detected no reaction center assembly complexes, indicating that synthesis was almost completely inhibited for all Chl-proteins, including the D1 and D2 proteins.

Indexed as

Gene Expression Regulation, EnzymologicBacterial ProteinsCell MembraneChlorophyllElectrophoresis, Gel, Two-DimensionalElectrophoresis, Polyacrylamide GelEnzyme ActivationGene Expression Regulation, PlantLightOxidoreductases Acting on CH-CH Group DonorsPhenotypePhotosystem II Protein ComplexPhotosystem I Protein ComplexPhototrophic ProcessesProtein BindingProtochlorophyllideBacterial ProteinsChlorophyllOxidoreductases Acting on CH-CH Group DonorsPhotosystem II Protein ComplexPhotosystem I Protein ComplexProtochlorophyllideprotochlorophyllide reductase

Identifiers

PMID23011568
OpenAlexW2028402893

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.