Publication Information
Xu et al., 2017
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Abstract
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.
Xu SL(1)(2), Chalkley RJ(2), Maynard JC(2), Wang W(3), Ni W(4)(5), Jiang X(6),
Shin K(3), Cheng L(3), Savage D(1), Hühmer AF(6), Burlingame AL(7), Wang ZY(8).
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.
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.
DOI: 10.1073/pnas.1610452114
PMCID: PMC5338445
PMID: 28154133 [Indexed for MEDLINE]
Conflict of interest statement: The authors declare no conflict of interest.
