Evidence map›Paper›PMID 26184543›Full record

ArticleNature communications2015

Downregulation of N-terminal acetylation triggers ABA-mediated drought responses in Arabidopsis.

Eric Linster, Iwona Stephan, Willy V Bienvenut, Jodi Maple-Grødem, Line M Myklebust, Monika Huber, Michael Reichelt, Carsten Sticht, Simon Geir Møller, Thierry Meinnel and 4 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
5.7field-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

72 citing papers in PubMed, 136 citations in OpenAlex.

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12 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 6 institutions in 4 countries.

Eric Linster1] Centre for Organismal Studies, University of Heidelberg, Heidelberg 69120, Germany [2] Hartmut Hoffmann-Berling International Graduate School, University of Heidelberg, Heidelberg 69120, Germany.
Iwona StephanCentre for Organismal Studies, University of Heidelberg, Heidelberg 69120, Germany.
Willy V BienvenutInstitute of Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Bâtiment 21, 1 avenue de la Terrasse, Gif-sur-Yvette F-91198, France.
Jodi Maple-GrødemCenter for Organelle Research, University of Stavanger, Stavanger N-4036, Norway.
Line M MyklebustDepartment of Molecular Biology, University of Bergen, Bergen N-5020, Norway.
Monika Huber1] Centre for Organismal Studies, University of Heidelberg, Heidelberg 69120, Germany [2] Hartmut Hoffmann-Berling International Graduate School, University of Heidelberg, Heidelberg 69120, Germany.
Michael ReicheltMax Planck institute for Chemical Ecology, Jena 07745, Germany.
Carsten StichtCenter for Medical Research, Mannheim 68167, Germany.
Simon Geir Møller1] Center for Organelle Research, University of Stavanger, Stavanger N-4036, Norway [2] Department of Biological Sciences, St John's University, New York, New York 11439, USA [3] Norwegian Centre for Movement Disorders, Stavanger University Hospital, Stavanger 4068, Norway.
Thierry MeinnelInstitute of Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Bâtiment 21, 1 avenue de la Terrasse, Gif-sur-Yvette F-91198, France.
Thomas Arnesen1] Department of Molecular Biology, University of Bergen, Bergen N-5020, Norway [2] Department of Surgery, Haukeland University Hospital, Bergen N-5021, Norway.
Carmela GiglioneInstitute of Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Bâtiment 21, 1 avenue de la Terrasse, Gif-sur-Yvette F-91198, France.
Rüdiger HellCentre for Organismal Studies, University of Heidelberg, Heidelberg 69120, Germany.
Markus WirtzCentre for Organismal Studies, University of Heidelberg, Heidelberg 69120, Germany.
Heidelberg University · DEInstitut de Biologie Intégrative de la Cellule · FRUniversity of Bergen · NOStavanger University Hospital · NOUniversity Medical Centre Mannheim · DEUniversity of Stavanger · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

N-terminal acetylation (NTA) catalysed by N-terminal acetyltransferases (Nats) is among the most common protein modifications in eukaryotes, but its significance is still enigmatic. Here we characterize the plant NatA complex and reveal evolutionary conservation of NatA biochemical properties in higher eukaryotes and uncover specific and essential functions of NatA for development, biosynthetic pathways and stress responses in plants. We show that NTA decreases significantly after drought stress, and NatA abundance is rapidly downregulated by the phytohormone abscisic acid. Accordingly, transgenic downregulation of NatA induces the drought stress response and results in strikingly drought resistant plants. Thus, we propose that NTA by the NatA complex acts as a cellular surveillance mechanism during stress and that imprinting of the proteome by NatA is an important switch for the control of metabolism, development and cellular stress responses downstream of abscisic acid.

Indexed as

ArabidopsisDroughtsGene Expression Regulation, PlantAbscisic AcidAcetylationArabidopsis ProteinsDown-RegulationEscherichia coliHEK293 CellsHumansN-Terminal Acetyltransferase AOrganisms, Genetically ModifiedReal-Time Polymerase Chain ReactionStress, PhysiologicalAbscisic AcidArabidopsis ProteinsN-Terminal Acetyltransferase A

Identifiers

PMID26184543
PMCPMC4530475
OpenAlexW1954288236

What OpenQuestion holds

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LicenceCC BY
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.