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Identification and analysis of the acetylated status of poplar proteins reveals analogous N-terminal protein processing mechanisms with other eukaryotes.

Identifieur interne : 002645 ( Main/Exploration ); précédent : 002644; suivant : 002646

Identification and analysis of the acetylated status of poplar proteins reveals analogous N-terminal protein processing mechanisms with other eukaryotes.

Auteurs : Chang-Cai Liu [République populaire de Chine] ; Hang-Yong Zhu ; Xiu-Mei Dong ; De-Li Ning ; Hong-Xia Wang ; Wei-Hua Li ; Chuan-Ping Yang ; Bai-Chen Wang

Source :

RBID : pubmed:23536812

Descripteurs français

English descriptors

Abstract

BACKGROUND

The N-terminal protein processing mechanism (NPM) including N-terminal Met excision (NME) and N-terminal acetylation (N(α)-acetylation) represents a common protein co-translational process of some eukaryotes. However, this NPM occurred in woody plants yet remains unknown.

METHODOLOGY/PRINCIPAL FINDINGS

To reveal the NPM in poplar, we investigated the N(α)-acetylation status of poplar proteins during dormancy by combining tandem mass spectrometry with TiO2 enrichment of acetylated peptides. We identified 58 N-terminally acetylated (N(α)-acetylated) proteins. Most proteins (47, >81%) are subjected to N(α)-acetylation following the N-terminal removal of Met, indicating that N(α)-acetylation and NME represent a common NPM of poplar proteins. Furthermore, we confirm that poplar shares the analogous NME and N(α)-acetylation (NPM) to other eukaryotes according to analysis of N-terminal features of these acetylated proteins combined with genome-wide identification of the involving methionine aminopeptidases (MAPs) and N-terminal acetyltransferase (Nat) enzymes in poplar. The N(α)-acetylated reactions and the involving enzymes of these poplar proteins are also identified based on those of yeast and human, as well as the subcellular location information of these poplar proteins.

CONCLUSIONS/SIGNIFICANCE

This study represents the first extensive investigation of N(α)-acetylation events in woody plants, the results of which will provide useful resources for future unraveling the regulatory mechanisms of N(α)-acetylation of proteins in poplar.


DOI: 10.1371/journal.pone.0058681
PubMed: 23536812
PubMed Central: PMC3594182


Affiliations:


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Le document en format XML

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<term>Acetylation (MeSH)</term>
<term>Amidohydrolases (metabolism)</term>
<term>Amino Acid Sequence (MeSH)</term>
<term>Aminopeptidases (classification)</term>
<term>Aminopeptidases (genetics)</term>
<term>Aminopeptidases (metabolism)</term>
<term>Arabidopsis (genetics)</term>
<term>Arabidopsis (metabolism)</term>
<term>Genome, Plant (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>N-Terminal Acetyltransferases (metabolism)</term>
<term>Phylogeny (MeSH)</term>
<term>Plant Proteins (metabolism)</term>
<term>Populus (enzymology)</term>
<term>Populus (genetics)</term>
<term>Populus (metabolism)</term>
<term>Position-Specific Scoring Matrices (MeSH)</term>
<term>Protein Processing, Post-Translational (MeSH)</term>
<term>Sequence Alignment (MeSH)</term>
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<term>Acétylation (MeSH)</term>
<term>Alignement de séquences (MeSH)</term>
<term>Amidohydrolases (métabolisme)</term>
<term>Aminopeptidases (classification)</term>
<term>Aminopeptidases (génétique)</term>
<term>Aminopeptidases (métabolisme)</term>
<term>Arabidopsis (génétique)</term>
<term>Arabidopsis (métabolisme)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Génome végétal (MeSH)</term>
<term>Matrices de scores (MeSH)</term>
<term>Maturation post-traductionnelle des protéines (MeSH)</term>
<term>N-terminal acetyltransferases (métabolisme)</term>
<term>Phylogenèse (MeSH)</term>
<term>Populus (enzymologie)</term>
<term>Populus (génétique)</term>
<term>Populus (métabolisme)</term>
<term>Protéines végétales (métabolisme)</term>
<term>Séquence d'acides aminés (MeSH)</term>
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<term>Aminopeptidases</term>
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<term>Aminopeptidases</term>
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<term>Amidohydrolases</term>
<term>Aminopeptidases</term>
<term>N-Terminal Acetyltransferases</term>
<term>Plant Proteins</term>
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<term>Aminopeptidases</term>
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<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr">
<term>Populus</term>
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<term>Populus</term>
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<term>Populus</term>
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<term>Aminopeptidases</term>
<term>Arabidopsis</term>
<term>Populus</term>
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<term>Populus</term>
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<term>Amidohydrolases</term>
<term>Aminopeptidases</term>
<term>Arabidopsis</term>
<term>N-terminal acetyltransferases</term>
<term>Populus</term>
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<term>Acetylation</term>
<term>Amino Acid Sequence</term>
<term>Genome, Plant</term>
<term>Molecular Sequence Data</term>
<term>Phylogeny</term>
<term>Position-Specific Scoring Matrices</term>
<term>Protein Processing, Post-Translational</term>
<term>Sequence Alignment</term>
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<term>Acétylation</term>
<term>Alignement de séquences</term>
<term>Données de séquences moléculaires</term>
<term>Génome végétal</term>
<term>Matrices de scores</term>
<term>Maturation post-traductionnelle des protéines</term>
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<b>BACKGROUND</b>
</p>
<p>The N-terminal protein processing mechanism (NPM) including N-terminal Met excision (NME) and N-terminal acetylation (N(α)-acetylation) represents a common protein co-translational process of some eukaryotes. However, this NPM occurred in woody plants yet remains unknown.</p>
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<p>
<b>METHODOLOGY/PRINCIPAL FINDINGS</b>
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<p>To reveal the NPM in poplar, we investigated the N(α)-acetylation status of poplar proteins during dormancy by combining tandem mass spectrometry with TiO2 enrichment of acetylated peptides. We identified 58 N-terminally acetylated (N(α)-acetylated) proteins. Most proteins (47, >81%) are subjected to N(α)-acetylation following the N-terminal removal of Met, indicating that N(α)-acetylation and NME represent a common NPM of poplar proteins. Furthermore, we confirm that poplar shares the analogous NME and N(α)-acetylation (NPM) to other eukaryotes according to analysis of N-terminal features of these acetylated proteins combined with genome-wide identification of the involving methionine aminopeptidases (MAPs) and N-terminal acetyltransferase (Nat) enzymes in poplar. The N(α)-acetylated reactions and the involving enzymes of these poplar proteins are also identified based on those of yeast and human, as well as the subcellular location information of these poplar proteins.</p>
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<b>CONCLUSIONS/SIGNIFICANCE</b>
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<p>This study represents the first extensive investigation of N(α)-acetylation events in woody plants, the results of which will provide useful resources for future unraveling the regulatory mechanisms of N(α)-acetylation of proteins in poplar.</p>
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