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

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:
 [1] ;  [2] ;  [2] ;  [3] ;  [4] ;  [5] ;  [3] ;  [3] ;  [6] ;  [5] ;  [7] ;  [8]
  1. Carnegie Inst. for Science, Stanford, CA (United States); Univ. of California, San Francisco, CA (United States)
  2. Univ. of California, San Francisco, CA (United States)
  3. Fujian Agriculture and Forestry Univ., Fuzhou (China)
  4. Univ. of California, Berkeley, CA (United States); Plant Gene Expression Center, Albany, CA (United States)
  5. Thermo Fisher Scientific, San Jose, CA (United States)
  6. Carnegie Inst. for Science, Stanford, CA (United States)
  7. Univ. of California, San Francisco, CA (United States); Univ. of Minnesota, St. Paul, MN (United States)
  8. Carnegie Inst. for Science, Stanford, CA (United States); Univ. of Minnesota, St. Paul, MN (United States)
Publication Date:
Grant/Contract Number:
FG02-08ER15973
Type:
Published Article
Journal Name:
Proceedings of the National Academy of Sciences of the United States of America
Additional Journal Information:
Journal Volume: 114; Journal Issue: 8; Journal ID: ISSN 0027-8424
Publisher:
National Academy of Sciences, Washington, DC (United States)
Research Org:
Carnegie Inst. of Washington, Washington, DC (United States)
Sponsoring Org:
USDOE
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; O-GlcNAcylation; proteomics; plant; Arabidopsis; phosphorylation
OSTI Identifier:
1342414
Alternate Identifier(s):
OSTI ID: 1464940

Xu, Shou -Ling, Chalkley, Robert J., Maynard, Jason C., Wang, Wenfei, Ni, Weimin, Jiang, Xiaoyue, Shin, Kihye, Cheng, Ling, Savage, Dasha, Huhmer, 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., 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, Huhmer, 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. 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, Huhmer, Andreas F. R., Burlingame, Alma L., and Wang, Zhi -Yong. 2017. "Proteomic analysis reveals O-GlcNAc modification on proteins with key regulatory functions in Arabidopsis". United States. doi: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 Huhmer, 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 = {2017},
month = {2}
}