Evidence map›Paper›PMID 24872381›Full record

ArticlePlant physiology2014

Lipoate-Protein Ligase and Octanoyltransferase Are Essential for Protein Lipoylation in Mitochondria of Arabidopsis.

Ralph Ewald, Christiane Hoffmann, Alexandra Florian, Ekkehard Neuhaus, Alisdair R Fernie, Hermann Bauwe

Open access · hybridAbstract 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 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

17 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Lipoic acid attachment to proteins: stimulating new developments.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  4. Article
  5. Article
  6. Article
  7. Characterization ofFrontiers in plant science · 2021
    Article
  8. Article
  9. Article
  10. Functional Identification and Structural Analysis of a New Lipoate Protein Ligase inFrontiers in cellular and infection microbiology · 2020
    Article
  11. Article
  12. Article
  13. Roles and maturation of iron-sulfur proteins in plastids.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018
    Review
  14. Lipoic acid metabolism and mitochondrial redox regulation.The Journal of biological chemistry · 2018
    Review
  15. Article
  16. Review
  17. Article
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

6 authors at 3 institutions in 1 country.

Ralph EwaldDepartment of Plant Physiology, University of Rostock, D-18059 Rostock, Germany (R.E., H.B.);Department of Plant Physiology, University of Kaiserslautern, D-67663 Kaiserslautern, Germany (C.H., E.N.); andMax-Planck-Institut für Molekulare Pflanzenphysiologie, 14476 Potsdam-Golm, Germany (A.F., A.R.F.).
Christiane HoffmannDepartment of Plant Physiology, University of Rostock, D-18059 Rostock, Germany (R.E., H.B.);Department of Plant Physiology, University of Kaiserslautern, D-67663 Kaiserslautern, Germany (C.H., E.N.); andMax-Planck-Institut für Molekulare Pflanzenphysiologie, 14476 Potsdam-Golm, Germany (A.F., A.R.F.).
Alexandra FlorianDepartment of Plant Physiology, University of Rostock, D-18059 Rostock, Germany (R.E., H.B.);Department of Plant Physiology, University of Kaiserslautern, D-67663 Kaiserslautern, Germany (C.H., E.N.); andMax-Planck-Institut für Molekulare Pflanzenphysiologie, 14476 Potsdam-Golm, Germany (A.F., A.R.F.).
Ekkehard NeuhausDepartment of Plant Physiology, University of Rostock, D-18059 Rostock, Germany (R.E., H.B.);Department of Plant Physiology, University of Kaiserslautern, D-67663 Kaiserslautern, Germany (C.H., E.N.); andMax-Planck-Institut für Molekulare Pflanzenphysiologie, 14476 Potsdam-Golm, Germany (A.F., A.R.F.).
Alisdair R FernieDepartment of Plant Physiology, University of Rostock, D-18059 Rostock, Germany (R.E., H.B.);Department of Plant Physiology, University of Kaiserslautern, D-67663 Kaiserslautern, Germany (C.H., E.N.); andMax-Planck-Institut für Molekulare Pflanzenphysiologie, 14476 Potsdam-Golm, Germany (A.F., A.R.F.).
Hermann BauweDepartment of Plant Physiology, University of Rostock, D-18059 Rostock, Germany (R.E., H.B.);Department of Plant Physiology, University of Kaiserslautern, D-67663 Kaiserslautern, Germany (C.H., E.N.); andMax-Planck-Institut für Molekulare Pflanzenphysiologie, 14476 Potsdam-Golm, Germany (A.F., A.R.F.) hermann.bauwe@uni-rostock.de.
Max Planck Institute of Molecular Plant Physiology · DEUniversity of Kaiserslautern · DEUniversity of Rostock · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Prosthetic lipoyl groups are required for the function of several essential multienzyme complexes, such as pyruvate dehydrogenase (PDH), α-ketoglutarate dehydrogenase (KGDH), and the glycine cleavage system (glycine decarboxylase [GDC]). How these proteins are lipoylated has been extensively studied in prokaryotes and yeast (Saccharomyces cerevisiae), but little is known for plants. We earlier reported that mitochondrial fatty acid synthesis by ketoacyl-acyl carrier protein synthase is not vital for protein lipoylation in Arabidopsis (Arabidopsis thaliana) and does not play a significant role in roots. Here, we identify Arabidopsis lipoate-protein ligase (AtLPLA) as an essential mitochondrial enzyme that uses octanoyl-nucleoside monophosphate and possibly other donor substrates for the octanoylation of mitochondrial PDH-E2 and GDC H-protein; it shows no reactivity with bacterial and possibly plant KGDH-E2. The octanoate-activating enzyme is unknown, but we assume that it uses octanoyl moieties provided by mitochondrial β-oxidation. AtLPLA is essential for the octanoylation of PDH-E2, whereas GDC H-protein can optionally also be octanoylated by octanoyltransferase (LIP2) using octanoyl chains provided by mitochondrial ketoacyl-acyl carrier protein synthase to meet the high lipoate requirement of leaf mesophyll mitochondria. Similar to protein lipoylation in yeast, LIP2 likely also transfers octanoyl groups attached to the H-protein to KGDH-E2 but not to PDH-E2, which is exclusively octanoylated by LPLA. We suggest that LPLA and LIP2 together provide a basal protein lipoylation network to plants that is similar to that in other eukaryotes.

Identifiers

PMID24872381
PMCPMC4081350
OpenAlexW2052034580

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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.