Evidence map›Paper›PMID 25800516›Full record

ArticlePhotosynthesis research2015

Characterization of a Synechocystis sp. PCC 6803 double mutant lacking the CyanoP and Ycf48 proteins of Photosystem II.

Simon A Jackson, Julian J Eaton-Rye

Abstract read
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Article in Photosynthesis research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
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

7 citing papers in PubMed.

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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

2 authors.

Simon A JacksonDepartment of Biochemistry, University of Otago, Dunedin, 9016, New Zealand.
Julian J Eaton-Rye

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Homologs of the Photosystem II (PS II) subunit PsbP are found in plants, algae, and cyanobacteria. In higher plants, PsbP is associated with mature PS II centers, but in cyanobacteria, the homologous CyanoP protein appears sub-stoichiometric to PS II. We have investigated the role of CyanoP by characterizing knockout mutants of the cyanobacterium Synechocystis sp. PCC 6803. Removal of CyanoP resulted in changes to phycobilisome coupling and energy transfer to PS II, but the function of PS II itself remained similar to wild type. We therefore investigated the hypothesis that CyanoP is involved in the biogenesis or repair of PS II by creating a double mutant lacking both CyanoP and the PS II assembly factor Ycf48. This strain exhibited an additive reduction in the amplitude of variable chlorophyll a fluorescence induction relative to either of the single mutants but displayed increased oxygen evolution, slight increases in PS II monomer and dimer levels, and a reduction in accumulation of an early PS II assembly complex containing CP47, compared to the ΔYcf48 strain.

Indexed as

Bacterial ProteinsChlorophyllChlorophyll AFluorescenceGene Knockout TechniquesMutationOxygenPhotosystem II Protein ComplexPhycobilisomesSynechocystisThylakoidsBacterial ProteinsChlorophyllChlorophyll AOxygenPhotosystem II Protein ComplexPhycobilisomes

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What OpenQuestion holds

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Registered trials

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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.