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

<h4>Background</h4>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 unkno...

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Autores principales:	Chang-Cai Liu, Hang-Yong Zhu, Xiu-Mei Dong, De-Li Ning, Hong-Xia Wang, Wei-Hua Li, Chuan-Ping Yang, Bai-Chen Wang
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/26a126acf0b342baaa9c9f704c4c9c3e
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spelling	oai:doaj.org-article:26a126acf0b342baaa9c9f704c4c9c3e2021-11-18T07:53:57ZIdentification and analysis of the acetylated status of poplar proteins reveals analogous N-terminal protein processing mechanisms with other eukaryotes.1932-620310.1371/journal.pone.0058681https://doaj.org/article/26a126acf0b342baaa9c9f704c4c9c3e2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23536812/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>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.<h4>Methodology/principal findings</h4>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.<h4>Conclusions/significance</h4>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.Chang-Cai LiuHang-Yong ZhuXiu-Mei DongDe-Li NingHong-Xia WangWei-Hua LiChuan-Ping YangBai-Chen WangPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 3, p e58681 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Chang-Cai Liu Hang-Yong Zhu Xiu-Mei Dong De-Li Ning Hong-Xia Wang Wei-Hua Li Chuan-Ping Yang Bai-Chen Wang Identification and analysis of the acetylated status of poplar proteins reveals analogous N-terminal protein processing mechanisms with other eukaryotes.
description	<h4>Background</h4>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.<h4>Methodology/principal findings</h4>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.<h4>Conclusions/significance</h4>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.
format	article
author	Chang-Cai Liu Hang-Yong Zhu Xiu-Mei Dong De-Li Ning Hong-Xia Wang Wei-Hua Li Chuan-Ping Yang Bai-Chen Wang
author_facet	Chang-Cai Liu Hang-Yong Zhu Xiu-Mei Dong De-Li Ning Hong-Xia Wang Wei-Hua Li Chuan-Ping Yang Bai-Chen Wang
author_sort	Chang-Cai Liu
title	Identification and analysis of the acetylated status of poplar proteins reveals analogous N-terminal protein processing mechanisms with other eukaryotes.
title_short	Identification and analysis of the acetylated status of poplar proteins reveals analogous N-terminal protein processing mechanisms with other eukaryotes.
title_full	Identification and analysis of the acetylated status of poplar proteins reveals analogous N-terminal protein processing mechanisms with other eukaryotes.
title_fullStr	Identification and analysis of the acetylated status of poplar proteins reveals analogous N-terminal protein processing mechanisms with other eukaryotes.
title_full_unstemmed	Identification and analysis of the acetylated status of poplar proteins reveals analogous N-terminal protein processing mechanisms with other eukaryotes.
title_sort	identification and analysis of the acetylated status of poplar proteins reveals analogous n-terminal protein processing mechanisms with other eukaryotes.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/26a126acf0b342baaa9c9f704c4c9c3e
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Identification and analysis of the acetylated status of poplar proteins reveals analogous N-terminal protein processing mechanisms with other eukaryotes.

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