PXD036527

PXD036527 is an original dataset announced via ProteomeXchange.

Title	Chemoproteomic profiling of O-GlcNAcylated proteins and identification of O-GlcNAc transferases in rice
Description	O-linked β-N-acetylglucosaminylation (O-GlcNAcylation) is a ubiquitous posttranslational modification occurring in both animals and plants. Thousands of proteins along with their O-GlcNAcylation sites have been identified in various animal systems, yet the O-GlcNAcylated proteomes in plants remain poorly understood. Here, we report a large-scale profiling of protein O-GlcNAcylation in a site-specific manner in rice. We first established the metabolic glycan labeling strategy (MGL) with N-azidoacetylgalactosamine (GalNAz) in rice seedlings, which enabled incorporation of azides as a bioorthogonal handle into O-GlcNAc. By conjugation of the azide-incorporated O-GlcNAc with alkyne-biotin containing a cleavable linker via click chemistry, O-GlcNAcylated proteins were selectively enriched for mass spectrometry (MS) analysis. A total of 1,591 unambiguous O-GlcNAcylation sites distributed on 709 O-GlcNAcylated proteins were identified. Additionally, 102 O-GlcNAcylated proteins were identified with their O-GlcNAcylation sites located within a serine/threonine-enriched peptide, causing ambiguous site assignment. The identified O-GlcNAcylated proteins are involved in multiple biological processes such as transcription, translation and plant hormone signaling. Furthermore, we discovered two O-GlcNAc transferases (OsOGTs) in rice. By expressing OsOGTs in Escherichia coli and Nicotiana benthamiana leaves, we confirmed their OGT enzymatic activities and used them to validate the identified rice O-GlcNAcylated proteins. Our dataset provides a valuable resource for studying O-GlcNAc biology in rice, and the MGL method should facilitate the identification of O-GlcNAcylated proteins in various plants.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_08:46:01.485.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Cong Lei
SpeciesList	scientific name: Oryza sativa (Rice); NCBI TaxID: 4530;
ModificationList	carbamoylated residue; phosphorylated residue; acetylated residue; monohydroxylated residue; complex glycosylation
Instrument	Orbitrap Fusion Lumos; LTQ Orbitrap Elite

Revision	Datetime	Status	ChangeLog Entry
0	2022-09-05 09:47:35	ID requested
1	2023-05-10 09:20:38	announced
⏵ 2	2023-11-14 08:46:02	announced	2023-11-14: Updated project metadata.

Li X, Lei C, Song Q, Bai L, Cheng B, Qin K, Li X, Ma B, Wang B, Zhou W, Chen X, Li J, Chemoproteomic profiling of O-GlcNAcylated proteins and identification of O-GlcNAc transferases in rice. Plant Biotechnol J, 21(4):742-753(2023) [pubmed]

submitter keyword: O-GlcNAcylation, HCD pd EThcD, metabolic glycan labeling, plant glycobiology.,rice, chemoproteomic

Jiayang Li
contact affiliation	State Key Laboratory of Plant Genomics and National Center for Plant Gene Research, Institute of Genetics and Developmental Biology, Innovation Academy for Seed Design, Chinese Academy of Sciences, Beijing 100101, China
contact email	jyli@genetics.ac.cn
lab head
Cong Lei
contact affiliation	Peking University
contact email	conglei@pku.edu.cn
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2023/05/PXD036527

PRIDE project URI

• PRIDE
  1. PXD036527
     1. Label: PRIDE project
     2. Name: Chemoproteomic profiling of O-GlcNAcylated proteins and identification of O-GlcNAc transferases in rice