Evidence map›Paper›PMID 25951519›Full record

ArticleProteomics2015

Molecular identification and functional characterization of the first Nα-acetyltransferase in plastids by global acetylome profiling.

Trinh V Dinh, Willy V Bienvenut, Eric Linster, Anna Feldman-Salit, Vincent A Jung, Thierry Meinnel, Rüdiger Hell, Carmela Giglione, Markus Wirtz

Open access · hybridAbstract read
In one paragraph

Article in Proteomics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

53 citing papers in PubMed, 104 citations in OpenAlex.

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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

9 authors at 3 institutions in 2 countries.

Trinh V DinhDepartment of Plant Molecular Biology, Centre for Organismal Studies, University of Heidelberg, Heidelberg, Germany.
Willy V BienvenutInstitute of Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Gif-sur-Yvette, France.
Eric LinsterDepartment of Plant Molecular Biology, Centre for Organismal Studies, University of Heidelberg, Heidelberg, Germany.
Anna Feldman-SalitMolecular and Cellular Modeling Group, Heidelberg Institute for Theoretical Studies gGbmH, Heidelberg, Germany.
Vincent A JungInstitute of Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Gif-sur-Yvette, France.
Thierry MeinnelInstitute of Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Gif-sur-Yvette, France.
Rüdiger HellDepartment of Plant Molecular Biology, Centre for Organismal Studies, University of Heidelberg, Heidelberg, Germany.
Carmela GiglioneInstitute of Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Gif-sur-Yvette, France.
Markus WirtzDepartment of Plant Molecular Biology, Centre for Organismal Studies, University of Heidelberg, Heidelberg, Germany.
Centre National de la Recherche Scientifique · FRHeidelberg University · DEHeidelberg Institute for Theoretical Studies · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein N(α) -terminal acetylation represents one of the most abundant protein modifications of higher eukaryotes. In humans, six N(α) -acetyltransferases (Nats) are responsible for the acetylation of approximately 80% of the cytosolic proteins. N-terminal protein acetylation has not been evidenced in organelles of metazoans, but in higher plants is a widespread modification not only in the cytosol but also in the chloroplast. In this study, we identify and characterize the first organellar-localized Nat in eukaryotes. A primary sequence-based search in Arabidopsis thaliana revealed seven putatively plastid-localized Nats of which AT2G39000 (AtNAA70) showed the highest conservation of the acetyl-CoA binding pocket. The chloroplastic localization of AtNAA70 was demonstrated by transient expression of AtNAA70:YFP in Arabidopsis mesophyll protoplasts. Homology modeling uncovered a significant conservation of tertiary structural elements between human HsNAA50 and AtNAA70. The in vivo acetylation activity of AtNAA70 was demonstrated on a number of distinct protein N(α) -termini with a newly established global acetylome profiling test after expression of AtNAA70 in E. coli. AtNAA70 predominately acetylated proteins starting with M, A, S and T, providing an explanation for most protein N-termini acetylation events found in chloroplasts. Like HsNAA50, AtNAA70 displays N(ε) -acetyltransferase activity on three internal lysine residues. All MS data have been deposited in the ProteomeXchange with identifier PXD001947 (http://proteomecentral.proteomexchange.org/dataset/PXD001947).

Indexed as

AcetylationAmino Acid SequenceArabidopsisCloning, MolecularEscherichia coliGene ExpressionHumansModels, MolecularMolecular Sequence DataN-Terminal AcetyltransferasesPlastidsProtein ConformationProteomicsTandem Mass SpectrometryN-Terminal AcetyltransferasesArabidopsis thalianaAtNAA70ChloroplastNα-acetyltransferasePlant proteomics

Identifiers

PMID25951519
PMCPMC4692087
OpenAlexW1883668892

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.