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Title: Proteomic analysis reveals O-GlcNAc modification on proteins with key regulatory functions in Arabidopsis

Abstract

Genetic studies have shown essential functions of O-linked N-acetylglucosamine (O-GlcNAc) modification in plants. However, the proteins and sites subject to this posttranslational modification are largely unknown. Here, we report a large-scale proteomic identification of O-GlcNAc–modified proteins and sites in the model plant Arabidopsis thaliana. Using lectin weak affinity chromatography to enrich modified peptides, followed by mass spectrometry, we identified 971 O-GlcNAc–modified peptides belonging to 262 proteins. The modified proteins are involved in cellular regulatory processes, including transcription, translation, epigenetic gene regulation, and signal transduction. Many proteins have functions in developmental and physiological processes specific to plants, such as hormone responses and flower development. Mass spectrometric analysis of phosphopeptides from the same samples showed that a large number of peptides could be modified by either O-GlcNAcylation or phosphorylation, but cooccurrence of the two modifications in the same peptide molecule was rare. Furthermore, our study generates a snapshot of the O-GlcNAc modification landscape in plants, indicating functions in many cellular regulation pathways and providing a powerful resource for further dissecting these functions at the molecular level.

Authors:
; ; ; ; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
Carnegie Inst. of Washington, Washington, DC (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1342414
Alternate Identifier(s):
OSTI ID: 1464940
Grant/Contract Number:  
FG02-08ER15973
Resource Type:
Published Article
Journal Name:
Proceedings of the National Academy of Sciences of the United States of America
Additional Journal Information:
Journal Name: Proceedings of the National Academy of Sciences of the United States of America Journal Volume: 114 Journal Issue: 8; Journal ID: ISSN 0027-8424
Publisher:
National Academy of Sciences, Washington, DC (United States)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; O-GlcNAcylation; proteomics; plant; Arabidopsis; phosphorylation

Citation Formats

Xu, Shou-Ling, Chalkley, Robert J., Maynard, Jason C., Wang, Wenfei, Ni, Weimin, Jiang, Xiaoyue, Shin, Kihye, Cheng, Ling, Savage, Dasha, Hühmer, Andreas F. R., Burlingame, Alma L., and Wang, Zhi-Yong. Proteomic analysis reveals O-GlcNAc modification on proteins with key regulatory functions in Arabidopsis. United States: N. p., 2017. Web. doi:10.1073/pnas.1610452114.
Xu, Shou-Ling, Chalkley, Robert J., Maynard, Jason C., Wang, Wenfei, Ni, Weimin, Jiang, Xiaoyue, Shin, Kihye, Cheng, Ling, Savage, Dasha, Hühmer, Andreas F. R., Burlingame, Alma L., & Wang, Zhi-Yong. Proteomic analysis reveals O-GlcNAc modification on proteins with key regulatory functions in Arabidopsis. United States. https://doi.org/10.1073/pnas.1610452114
Xu, Shou-Ling, Chalkley, Robert J., Maynard, Jason C., Wang, Wenfei, Ni, Weimin, Jiang, Xiaoyue, Shin, Kihye, Cheng, Ling, Savage, Dasha, Hühmer, Andreas F. R., Burlingame, Alma L., and Wang, Zhi-Yong. Thu . "Proteomic analysis reveals O-GlcNAc modification on proteins with key regulatory functions in Arabidopsis". United States. https://doi.org/10.1073/pnas.1610452114.
@article{osti_1342414,
title = {Proteomic analysis reveals O-GlcNAc modification on proteins with key regulatory functions in Arabidopsis},
author = {Xu, Shou-Ling and Chalkley, Robert J. and Maynard, Jason C. and Wang, Wenfei and Ni, Weimin and Jiang, Xiaoyue and Shin, Kihye and Cheng, Ling and Savage, Dasha and Hühmer, Andreas F. R. and Burlingame, Alma L. and Wang, Zhi-Yong},
abstractNote = {Genetic studies have shown essential functions of O-linked N-acetylglucosamine (O-GlcNAc) modification in plants. However, the proteins and sites subject to this posttranslational modification are largely unknown. Here, we report a large-scale proteomic identification of O-GlcNAc–modified proteins and sites in the model plant Arabidopsis thaliana. Using lectin weak affinity chromatography to enrich modified peptides, followed by mass spectrometry, we identified 971 O-GlcNAc–modified peptides belonging to 262 proteins. The modified proteins are involved in cellular regulatory processes, including transcription, translation, epigenetic gene regulation, and signal transduction. Many proteins have functions in developmental and physiological processes specific to plants, such as hormone responses and flower development. Mass spectrometric analysis of phosphopeptides from the same samples showed that a large number of peptides could be modified by either O-GlcNAcylation or phosphorylation, but cooccurrence of the two modifications in the same peptide molecule was rare. Furthermore, our study generates a snapshot of the O-GlcNAc modification landscape in plants, indicating functions in many cellular regulation pathways and providing a powerful resource for further dissecting these functions at the molecular level.},
doi = {10.1073/pnas.1610452114},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
number = 8,
volume = 114,
place = {United States},
year = {Thu Feb 02 00:00:00 EST 2017},
month = {Thu Feb 02 00:00:00 EST 2017}
}

Journal Article:
Free Publicly Available Full Text
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https://doi.org/10.1073/pnas.1610452114

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