Evidence map›Paper›PMID 24424322›Full record

ArticlePlant physiology2014

The Arabidopsis class II sirtuin is a lysine deacetylase and interacts with mitochondrial energy metabolism.

Ann-Christine König, Markus Hartl, Phuong Anh Pham, Miriam Laxa, Paul J Boersema, Anne Orwat, Ievgeniia Kalitventseva, Magdalena Plöchinger, Hans-Peter Braun, Dario Leister and 4 more

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 44 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed, 1 pooled it
6.3field-weighted citation impact, top 3% 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

44 citing papers in PubMed, 1 synthesis or guideline pooled it, 114 citations in OpenAlex.

  1. Pooled it
  2. Linking cellular metabolism to chromatin modifications in plants.Journal of integrative plant biology · 2026
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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

14 authors at 5 institutions in 1 country.

Ann-Christine KönigDepartment I of Biology, Ludwig Maximilians University Munich, Grosshaderner Strasse 2, 82152 Martinsried, Germany.
Markus Hartl
Phuong Anh Pham
Miriam Laxa
Paul J Boersema
Anne Orwat
Ievgeniia Kalitventseva
Magdalena Plöchinger
Hans-Peter Braun
Dario Leister
Matthias Mann
Andreas Wachter
Alisdair R Fernie
Iris Finkemeier
Ludwig-Maximilians-Universität München · DEMax Planck Institute of Biochemistry · DEMax Planck Institute of Molecular Plant Physiology · DELeibniz University Hannover · DEUniversity of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The posttranslational regulation of proteins by lysine (Lys) acetylation has recently emerged to occur not only on histones, but also on organellar proteins in plants and animals. In particular, the catalytic activities of metabolic enzymes have been shown to be regulated by Lys acetylation. The Arabidopsis (Arabidopsis thaliana) genome encodes two predicted sirtuin-type Lys deacetylases, of which only Silent Information Regulator2 homolog (SRT2) contains a predicted presequence for mitochondrial targeting. Here, we have investigated the function of SRT2 in Arabidopsis. We demonstrate that SRT2 functions as a Lys deacetylase in vitro and in vivo. We show that SRT2 resides predominantly at the inner mitochondrial membrane and interacts with a small number of protein complexes mainly involved in energy metabolism and metabolite transport. Several of these protein complexes, such as the ATP synthase and the ATP/ADP carriers, show an increase in Lys acetylation in srt2 loss-of-function mutants. The srt2 plants display no growth phenotype but rather a metabolic phenotype with altered levels in sugars, amino acids, and ADP contents. Furthermore, coupling of respiration to ATP synthesis is decreased in these lines, while the ADP uptake into mitochondria is significantly increased. Our results indicate that SRT2 is important in fine-tuning mitochondrial energy metabolism.

Indexed as

Energy MetabolismAcetylationAdenosine DiphosphateAdenosine TriphosphateAmino Acid SequenceArabidopsisArabidopsis ProteinsCarbon IsotopesCell RespirationGene Knockout TechniquesHistone DeacetylasesLysineMitochondriaMitochondrial MembranesMitochondrial ProteinsMolecular Sequence DataAdenosine DiphosphateAdenosine TriphosphateArabidopsis ProteinsCarbon IsotopesHistone DeacetylasesLysineMitochondrial ProteinsNADRNA, MessengerSirtuinsSRT2 protein, Arabidopsis

Identifiers

PMID24424322
PMCPMC3938629
OpenAlexW2158541299

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.