Evidence map›Paper›PMID 27208291›Full record

ArticlePlant physiology2016

Thylakoid-Bound FtsH Proteins Facilitate Proper Biosynthesis of Photosystem I.

Sari Järvi, Marjaana Suorsa, Luca Tadini, Aiste Ivanauskaite, Sanna Rantala, Yagut Allahverdiyeva, Dario Leister, Eva-Mari Aro

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

28 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
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  15. Impacts of Nitrogen Deficiency on Wheat (Frontiers in plant science · 2021
    Article
  16. Article
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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

8 authors at 2 institutions in 2 countries.

Sari JärviMolecular Plant Biology, Department of Biochemistry, University of Turku, FI-20520 Turku, Finland (S.J., M.S., A.I., S.R., Y.A., E.-M.A.); andPlant Molecular Biology (Botany), Department of Biology I, Ludwig-Maximilians-Universität München, 82152 Planegg-Martinsried, Germany (L.T., D.L.).ORCID 0000-0003-4235-9292
Marjaana SuorsaMolecular Plant Biology, Department of Biochemistry, University of Turku, FI-20520 Turku, Finland (S.J., M.S., A.I., S.R., Y.A., E.-M.A.); andPlant Molecular Biology (Botany), Department of Biology I, Ludwig-Maximilians-Universität München, 82152 Planegg-Martinsried, Germany (L.T., D.L.).ORCID 0000-0002-3821-0607
Luca TadiniMolecular Plant Biology, Department of Biochemistry, University of Turku, FI-20520 Turku, Finland (S.J., M.S., A.I., S.R., Y.A., E.-M.A.); andPlant Molecular Biology (Botany), Department of Biology I, Ludwig-Maximilians-Universität München, 82152 Planegg-Martinsried, Germany (L.T., D.L.).ORCID 0000-0003-2315-7695
Aiste IvanauskaiteMolecular Plant Biology, Department of Biochemistry, University of Turku, FI-20520 Turku, Finland (S.J., M.S., A.I., S.R., Y.A., E.-M.A.); andPlant Molecular Biology (Botany), Department of Biology I, Ludwig-Maximilians-Universität München, 82152 Planegg-Martinsried, Germany (L.T., D.L.).ORCID 0000-0002-1149-5243
Sanna RantalaMolecular Plant Biology, Department of Biochemistry, University of Turku, FI-20520 Turku, Finland (S.J., M.S., A.I., S.R., Y.A., E.-M.A.); andPlant Molecular Biology (Botany), Department of Biology I, Ludwig-Maximilians-Universität München, 82152 Planegg-Martinsried, Germany (L.T., D.L.).ORCID 0000-0001-8106-2657
Yagut AllahverdiyevaMolecular Plant Biology, Department of Biochemistry, University of Turku, FI-20520 Turku, Finland (S.J., M.S., A.I., S.R., Y.A., E.-M.A.); andPlant Molecular Biology (Botany), Department of Biology I, Ludwig-Maximilians-Universität München, 82152 Planegg-Martinsried, Germany (L.T., D.L.).ORCID 0000-0002-9262-1757
Dario LeisterMolecular Plant Biology, Department of Biochemistry, University of Turku, FI-20520 Turku, Finland (S.J., M.S., A.I., S.R., Y.A., E.-M.A.); andPlant Molecular Biology (Botany), Department of Biology I, Ludwig-Maximilians-Universität München, 82152 Planegg-Martinsried, Germany (L.T., D.L.).ORCID 0000-0003-1897-8421
Eva-Mari AroMolecular Plant Biology, Department of Biochemistry, University of Turku, FI-20520 Turku, Finland (S.J., M.S., A.I., S.R., Y.A., E.-M.A.); andPlant Molecular Biology (Botany), Department of Biology I, Ludwig-Maximilians-Universität München, 82152 Planegg-Martinsried, Germany (L.T., D.L.) evaaro@utu.fi.ORCID 0000-0002-2922-1435
University of Turku · FILudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thylakoid membrane-bound FtsH proteases have a well-characterized role in degradation of the photosystem II (PSII) reaction center protein D1 upon repair of photodamaged PSII. Here, we show that the Arabidopsis (Arabidopsis thaliana) var1 and var2 mutants, devoid of the FtsH5 and FtsH2 proteins, respectively, are capable of normal D1 protein turnover under moderate growth light intensity. Instead, they both demonstrate a significant scarcity of PSI complexes. It is further shown that the reduced level of PSI does not result from accelerated photodamage of the PSI centers in var1 or var2 under moderate growth light intensity. On the contrary, radiolabeling experiments revealed impaired synthesis of the PsaA/B reaction center proteins of PSI, which was accompanied by the accumulation of PSI-specific assembly factors. psaA/B transcript accumulation and translation initiation, however, occurred in var1 and var2 mutants as in wild-type Arabidopsis, suggesting problems in later stages of PsaA/B protein expression in the two var mutants. Presumably, the thylakoid membrane-bound FtsH5 and FtsH2 have dual functions in the maintenance of photosynthetic complexes. In addition to their function as a protease in the degradation of the photodamaged D1 protein, they also are required, either directly or indirectly, for early assembly of the PSI complexes.

Indexed as

ArabidopsisArabidopsis ProteinsATP-Dependent ProteasesElectron TransportLightMembrane ProteinsMetalloproteasesMutationPhotosynthesisPhotosystem II Protein ComplexPhotosystem I Protein ComplexProtein BindingProtein SubunitsProteolysisThylakoidsArabidopsis ProteinsAT2G30950 protein, ArabidopsisATP-Dependent ProteasesFtsH5 protein, ArabidopsisMembrane ProteinsMetalloproteasesPhotosystem II Protein ComplexPhotosystem I Protein ComplexProtein Subunits

Identifiers

PMID27208291
PMCPMC4902603
OpenAlexW2419536542

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.