Evidence map›Paper›PMID 19674969›Full record

ArticleThe Journal of biological chemistry2009

Multiple Rieske proteins enable short- and long-term light adaptation of Synechocystis sp. PCC 6803.

Yuichi Tsunoyama, Gábor Bernát, Nina G Dyczmons, Dirk Schneider, Matthias Rögner

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

10 citing papers in PubMed, 28 citations in OpenAlex.

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  7. The cytochrome bd respiratory oxygen reductases.Biochimica et biophysica acta · 2011
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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

5 authors at 3 institutions in 2 countries.

Yuichi TsunoyamaDepartment of Plant Biochemistry, Ruhr-University Bochum, 44780 Bochum, Germany; Division of Biology, Radioisotope Research Center, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
Gábor BernátDepartment of Plant Biochemistry, Ruhr-University Bochum, 44780 Bochum, Germany.
Nina G DyczmonsDepartment of Plant Biochemistry, Ruhr-University Bochum, 44780 Bochum, Germany.
Dirk SchneiderDepartment of Biochemistry and Molecular Biology, ZBMZ, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany.
Matthias RögnerDepartment of Plant Biochemistry, Ruhr-University Bochum, 44780 Bochum, Germany. Electronic address: Matthias.Roegner@rub.de.
Ruhr University Bochum · DEKyoto University · JPUniversity of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In contrast to eukaryotes, most cyanobacteria contain several isoforms of the Rieske iron-sulfur protein, PetC, resulting in heterogeneity in the composition of the cytochrome b(6)f complexes. Of three isoforms in the mesophilic cyanobacterium Synechocystis PCC 6803, PetC1 is the major Rieske protein in the cytochrome b(6)f complex, whereas the physiological function of PetC2 and PetC3 is still uncertain. Comparison of wild type and various petC-deficient strains under selected light conditions revealed distinct functional differences: high-light exposure of wild type cells resulted in a significantly enhanced petC2 transcript level, whereas a Delta petC1 mutant showed a low cytochrome b(6)f content, low electron flux, and a considerably increased accumulation of cytochrome-bd oxidase. In contrast to wild type and Delta petC1, Delta petC2 and Delta petC3 strains still grew fast under high-light conditions although all three Rieske proteins are required for maximal electron transport rates. Although the presence of PetC3 appears to be required for activation of the cyclic electron transport, state transitions were more effective in the absence of PetC2 and/or PetC3. In summary, our data suggest defined roles of the various PetC proteins in short- and long-term light adaptation.

Indexed as

Adaptation, PhysiologicalLightBacterial ProteinsChlorophyllCytochrome b6f ComplexElectron TransportElectron Transport Complex IIIGene Expression Regulation, BacterialOxidation-ReductionPhotosynthesisPhycocyaninProtein IsoformsProtein SubunitsSynechocystisallophycocyaninBacterial ProteinsChlorophyllCytochrome b6f ComplexElectron Transport Complex IIIPhycocyaninProtein IsoformsProtein SubunitsRieske iron-sulfur protein

Identifiers

PMID19674969
PMCPMC2788838
OpenAlexW2014656919

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.