Evidence map›Paper›PMID 22223895›Full record

ArticleMolecular & cellular proteomics : MCP2012

Comparative large scale characterization of plant versus mammal proteins reveals similar and idiosyncratic N-α-acetylation features.

Willy V Bienvenut, David Sumpton, Aude Martinez, Sergio Lilla, Christelle Espagne, Thierry Meinnel, Carmela Giglione

Abstract readComparative Study
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

104 citing papers in PubMed.

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  11. Posttranslational Regulation of Mammalian Sulfur Amino Acid Metabolism.International journal of molecular sciences · 2025
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44 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

7 authors.

Willy V BienvenutCNRS, Centre de Recherche de Gif, Institut des Sciences du Végétal, F-91198 Gif-sur-Yvette cedex, France.
David Sumpton
Aude Martinez
Sergio Lilla
Christelle Espagne
Thierry Meinnel
Carmela Giglione

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

N-terminal modifications play a major role in the fate of proteins in terms of activity, stability, or subcellular compartmentalization. Such modifications remain poorly described and badly characterized in proteomic studies, and only a few comparison studies among organisms have been made available so far. Recent advances in the field now allow the enrichment and selection of N-terminal peptides in the course of proteome-wide mass spectrometry analyses. These targeted approaches unravel as a result the extent and nature of the protein N-terminal modifications. Here, we aimed at studying such modifications in the model plant Arabidopsis thaliana to compare these results with those obtained from a human sample analyzed in parallel. We applied large scale analysis to compile robust conclusions on both data sets. Our data show strong convergence of the characterized modifications especially for protein N-terminal methionine excision, co-translational N-α-acetylation, or N-myristoylation between animal and plant kingdoms. Because of the convergence of both the substrates and the N-α-acetylation machinery, it was possible to identify the N-acetyltransferases involved in such modifications for a small number of model plants. Finally, a high proportion of nuclear-encoded chloroplast proteins feature post-translational N-α-acetylation of the mature protein after removal of the transit peptide. Unlike animals, plants feature in a dedicated pathway for post-translational acetylation of organelle-targeted proteins. The corresponding machinery is yet to be discovered.

Indexed as

Protein Processing, Post-TranslationalAcetylationAcetyltransferasesArabidopsis ProteinsCell LineChromatography, Ion ExchangeComputer SimulationHumansModels, BiologicalPeptide FragmentsPhylogenyProtein Structure, TertiaryProtein TransportProteomeTandem Mass SpectrometryAcetyltransferasesArabidopsis ProteinsPeptide FragmentsProteome

Identifiers

PMID22223895
PMCPMC3433923

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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.