Format

Send to

Choose Destination
Proc Natl Acad Sci U S A. 2017 Feb 21;114(8):E1536-E1543. doi: 10.1073/pnas.1610452114. Epub 2017 Feb 2.

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

Author information

1
Department of Plant Biology, Carnegie Institution for Science, Stanford, CA 94305.
2
Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94158.
3
Basic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
4
Department of Plant and Microbial Biology, University of California, Berkeley, CA, 94720.
5
Plant Gene Expression Center, United States Department of Agriculture/Agriculture Research Service, Albany, CA94710.
6
Thermo Fisher Scientific, San Jose, CA 95134.
7
Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94158; zywang24@stanford.edu alb@cgl.ucsf.edu.
8
Department of Plant Biology, Carnegie Institution for Science, Stanford, CA 94305; zywang24@stanford.edu alb@cgl.ucsf.edu.

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. 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.

KEYWORDS:

Arabidopsis; O-GlcNAcylation; phosphorylation; plant; proteomics

PMID:
28154133
PMCID:
PMC5338445
DOI:
10.1073/pnas.1610452114
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center