Evidence map›Paper›PMID 25301888›Full record

ArticlePlant physiology2014

Posttranslational modifications of FERREDOXIN-NADP+ OXIDOREDUCTASE in Arabidopsis chloroplasts.

Nina Lehtimäki, Minna M Koskela, Käthe M Dahlström, Eveliina Pakula, Minna Lintala, Martin Scholz, Michael Hippler, Guy T Hanke, Anne Rokka, Natalia Battchikova and 2 more

Abstract read
In one paragraph

Article in Plant physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

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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

13 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

12 authors.

Nina LehtimäkiMolecular Plant Biology, Department of Biochemistry, University of Turku, FI-20520 Turku, Finland (N.L., M.M.K., E.P., M.L., N.B., P.M.);Structural Bioinformatics Laboratory, Department of Biosciences, Åbo Akademi University, FI-20520 Turku, Finland (K.M.D., T.A.S.);Institute of Plant Biology and Biotechnology, Faculty of Biology, Westfälische Wilhelms-Universität Münster, DE-48143 Muenster, Germany (M.S., M.H.);Plant Physiology, Faculty of Biology and Chemistry, University of Osnabrück, DE-49076 Osnabruck, Germany (G.T.H.); andTurku Centre for Biotechnology, FI-20520 Turku, Finland (A.R.).
Minna M KoskelaMolecular Plant Biology, Department of Biochemistry, University of Turku, FI-20520 Turku, Finland (N.L., M.M.K., E.P., M.L., N.B., P.M.);Structural Bioinformatics Laboratory, Department of Biosciences, Åbo Akademi University, FI-20520 Turku, Finland (K.M.D., T.A.S.);Institute of Plant Biology and Biotechnology, Faculty of Biology, Westfälische Wilhelms-Universität Münster, DE-48143 Muenster, Germany (M.S., M.H.);Plant Physiology, Faculty of Biology and Chemistry, University of Osnabrück, DE-49076 Osnabruck, Germany (G.T.H.); andTurku Centre for Biotechnology, FI-20520 Turku, Finland (A.R.).
Käthe M DahlströmMolecular Plant Biology, Department of Biochemistry, University of Turku, FI-20520 Turku, Finland (N.L., M.M.K., E.P., M.L., N.B., P.M.);Structural Bioinformatics Laboratory, Department of Biosciences, Åbo Akademi University, FI-20520 Turku, Finland (K.M.D., T.A.S.);Institute of Plant Biology and Biotechnology, Faculty of Biology, Westfälische Wilhelms-Universität Münster, DE-48143 Muenster, Germany (M.S., M.H.);Plant Physiology, Faculty of Biology and Chemistry, University of Osnabrück, DE-49076 Osnabruck, Germany (G.T.H.); andTurku Centre for Biotechnology, FI-20520 Turku, Finland (A.R.).
Eveliina PakulaMolecular Plant Biology, Department of Biochemistry, University of Turku, FI-20520 Turku, Finland (N.L., M.M.K., E.P., M.L., N.B., P.M.);Structural Bioinformatics Laboratory, Department of Biosciences, Åbo Akademi University, FI-20520 Turku, Finland (K.M.D., T.A.S.);Institute of Plant Biology and Biotechnology, Faculty of Biology, Westfälische Wilhelms-Universität Münster, DE-48143 Muenster, Germany (M.S., M.H.);Plant Physiology, Faculty of Biology and Chemistry, University of Osnabrück, DE-49076 Osnabruck, Germany (G.T.H.); andTurku Centre for Biotechnology, FI-20520 Turku, Finland (A.R.).
Minna LintalaMolecular Plant Biology, Department of Biochemistry, University of Turku, FI-20520 Turku, Finland (N.L., M.M.K., E.P., M.L., N.B., P.M.);Structural Bioinformatics Laboratory, Department of Biosciences, Åbo Akademi University, FI-20520 Turku, Finland (K.M.D., T.A.S.);Institute of Plant Biology and Biotechnology, Faculty of Biology, Westfälische Wilhelms-Universität Münster, DE-48143 Muenster, Germany (M.S., M.H.);Plant Physiology, Faculty of Biology and Chemistry, University of Osnabrück, DE-49076 Osnabruck, Germany (G.T.H.); andTurku Centre for Biotechnology, FI-20520 Turku, Finland (A.R.).
Martin ScholzMolecular Plant Biology, Department of Biochemistry, University of Turku, FI-20520 Turku, Finland (N.L., M.M.K., E.P., M.L., N.B., P.M.);Structural Bioinformatics Laboratory, Department of Biosciences, Åbo Akademi University, FI-20520 Turku, Finland (K.M.D., T.A.S.);Institute of Plant Biology and Biotechnology, Faculty of Biology, Westfälische Wilhelms-Universität Münster, DE-48143 Muenster, Germany (M.S., M.H.);Plant Physiology, Faculty of Biology and Chemistry, University of Osnabrück, DE-49076 Osnabruck, Germany (G.T.H.); andTurku Centre for Biotechnology, FI-20520 Turku, Finland (A.R.).
Michael HipplerMolecular Plant Biology, Department of Biochemistry, University of Turku, FI-20520 Turku, Finland (N.L., M.M.K., E.P., M.L., N.B., P.M.);Structural Bioinformatics Laboratory, Department of Biosciences, Åbo Akademi University, FI-20520 Turku, Finland (K.M.D., T.A.S.);Institute of Plant Biology and Biotechnology, Faculty of Biology, Westfälische Wilhelms-Universität Münster, DE-48143 Muenster, Germany (M.S., M.H.);Plant Physiology, Faculty of Biology and Chemistry, University of Osnabrück, DE-49076 Osnabruck, Germany (G.T.H.); andTurku Centre for Biotechnology, FI-20520 Turku, Finland (A.R.).
Guy T HankeMolecular Plant Biology, Department of Biochemistry, University of Turku, FI-20520 Turku, Finland (N.L., M.M.K., E.P., M.L., N.B., P.M.);Structural Bioinformatics Laboratory, Department of Biosciences, Åbo Akademi University, FI-20520 Turku, Finland (K.M.D., T.A.S.);Institute of Plant Biology and Biotechnology, Faculty of Biology, Westfälische Wilhelms-Universität Münster, DE-48143 Muenster, Germany (M.S., M.H.);Plant Physiology, Faculty of Biology and Chemistry, University of Osnabrück, DE-49076 Osnabruck, Germany (G.T.H.); andTurku Centre for Biotechnology, FI-20520 Turku, Finland (A.R.).
Anne RokkaMolecular Plant Biology, Department of Biochemistry, University of Turku, FI-20520 Turku, Finland (N.L., M.M.K., E.P., M.L., N.B., P.M.);Structural Bioinformatics Laboratory, Department of Biosciences, Åbo Akademi University, FI-20520 Turku, Finland (K.M.D., T.A.S.);Institute of Plant Biology and Biotechnology, Faculty of Biology, Westfälische Wilhelms-Universität Münster, DE-48143 Muenster, Germany (M.S., M.H.);Plant Physiology, Faculty of Biology and Chemistry, University of Osnabrück, DE-49076 Osnabruck, Germany (G.T.H.); andTurku Centre for Biotechnology, FI-20520 Turku, Finland (A.R.).
Natalia BattchikovaMolecular Plant Biology, Department of Biochemistry, University of Turku, FI-20520 Turku, Finland (N.L., M.M.K., E.P., M.L., N.B., P.M.);Structural Bioinformatics Laboratory, Department of Biosciences, Åbo Akademi University, FI-20520 Turku, Finland (K.M.D., T.A.S.);Institute of Plant Biology and Biotechnology, Faculty of Biology, Westfälische Wilhelms-Universität Münster, DE-48143 Muenster, Germany (M.S., M.H.);Plant Physiology, Faculty of Biology and Chemistry, University of Osnabrück, DE-49076 Osnabruck, Germany (G.T.H.); andTurku Centre for Biotechnology, FI-20520 Turku, Finland (A.R.).
Tiina A SalminenMolecular Plant Biology, Department of Biochemistry, University of Turku, FI-20520 Turku, Finland (N.L., M.M.K., E.P., M.L., N.B., P.M.);Structural Bioinformatics Laboratory, Department of Biosciences, Åbo Akademi University, FI-20520 Turku, Finland (K.M.D., T.A.S.);Institute of Plant Biology and Biotechnology, Faculty of Biology, Westfälische Wilhelms-Universität Münster, DE-48143 Muenster, Germany (M.S., M.H.);Plant Physiology, Faculty of Biology and Chemistry, University of Osnabrück, DE-49076 Osnabruck, Germany (G.T.H.); andTurku Centre for Biotechnology, FI-20520 Turku, Finland (A.R.).
Paula MuloMolecular Plant Biology, Department of Biochemistry, University of Turku, FI-20520 Turku, Finland (N.L., M.M.K., E.P., M.L., N.B., P.M.);Structural Bioinformatics Laboratory, Department of Biosciences, Åbo Akademi University, FI-20520 Turku, Finland (K.M.D., T.A.S.);Institute of Plant Biology and Biotechnology, Faculty of Biology, Westfälische Wilhelms-Universität Münster, DE-48143 Muenster, Germany (M.S., M.H.);Plant Physiology, Faculty of Biology and Chemistry, University of Osnabrück, DE-49076 Osnabruck, Germany (G.T.H.); andTurku Centre for Biotechnology, FI-20520 Turku, Finland (A.R.) pmulo@utu.fi.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rapid responses of chloroplast metabolism and adjustments to photosynthetic machinery are of utmost importance for plants' survival in a fluctuating environment. These changes may be achieved through posttranslational modifications of proteins, which are known to affect the activity, interactions, and localization of proteins. Recent studies have accumulated evidence about the crucial role of a multitude of modifications, including acetylation, methylation, and glycosylation, in the regulation of chloroplast proteins. Both of the Arabidopsis (Arabidopsis thaliana) leaf-type FERREDOXIN-NADP(+) OXIDOREDUCTASE (FNR) isoforms, the key enzymes linking the light reactions of photosynthesis to carbon assimilation, exist as two distinct forms with different isoelectric points. We show that both AtFNR isoforms contain multiple alternative amino termini and undergo light-responsive addition of an acetyl group to the α-amino group of the amino-terminal amino acid of proteins, which causes the change in isoelectric point. Both isoforms were also found to contain acetylation of a conserved lysine residue near the active site, while no evidence for in vivo phosphorylation or glycosylation was detected. The dynamic, multilayer regulation of AtFNR exemplifies the complex regulatory network systems controlling chloroplast proteins by a range of posttranslational modifications, which continues to emerge as a novel area within photosynthesis research.

Indexed as

Protein Processing, Post-TranslationalAcetylationAmino Acid SequenceArabidopsisArabidopsis ProteinsChloroplastsFerredoxin-NADP ReductaseFerredoxinsGlycosylationIsoenzymesLightModels, StructuralMolecular Sequence DataNADPPhosphorylationPhotosynthesisArabidopsis ProteinsFerredoxin-NADP ReductaseFerredoxinsIsoenzymesNADP

Identifiers

PMID25301888
PMCPMC4256869

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