PXD022483

PXD022483 is an original dataset announced via ProteomeXchange.

Title	Global profiling of N-glycosylated proteins in the diatom Phaeodactylum tricornutum
Description	N-glycosylation is an important posttranslational modification in all eukaryotes, but little is known about the N-glycoproteomes in microalgal systems. Here, N-glycoproteome of the model diatom Phaeodactylum tricornutum was unveiled. Totally, 893 different N-glycosylated sites from 649 proteins were identified from P. tricornutum. The new synthesized N-glycans were principally transferred to asparagine residues within the conserved N-X-S/T (where X is a residue other than proline) sequence of nascent polypeptide chains. Functional annotation of N-glycosylated proteins showed that 70% N-glycoproteins were involved in vesicular transport and posttranslational modification, protein turnover, chaperones, indicating the N-glycosylation was important for these functions. Of the all identified N-glycoproteins 45.3% were predicted to localize on chloroplast, which implied the widespread regulatory role of N-glycosylation in chloroplast. Furthermore, the enrichment results of N-glycoproteins indicated that compared to ‘Cellular component’ and ‘Biological process’ categories proteins related with the ‘Molecular function’ category were more prone to be N-glycosylated. And it was speculated that N-glycosylation played a vital regulatory role in catalytic activity of enzymes and metabolism processes of many small molecules. 47% of all enriched proteins were related with metabolic pathways. The functional annotation and enrichment of N-glycoproteins suggested that N-glycoproteins participated in a variety of important metabolic pathways and perform different functions in P. tricornutum. 12 proteins involved in the ER quality control mechanism and ER- associated degradation pathway were identified as N-glycosylated proteins, indicating that the N-glycosylated modification was important for their functions in the protein N-glycosylation pathway. Additionally, some interacted glycoproteins were classified from this study, which provided valuable information for studying the functions of these glycoproteins. In the study, the identification of N-glycosylation on nascent proteins expands our understanding of this PTM at a proteomics scale and may facilitate the elucidation of the precise function of proteins in this model diatom.
HostingRepository	PRIDE
AnnounceDate	2021-11-03
AnnouncementXML	Submission_2021-11-03_05:55:24.833.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Xiaojuan Liu
SpeciesList	scientific name: Phaeodactylum tricornutum; NCBI TaxID: 2850;
ModificationList	N-glycosylated residue
Instrument	Q Exactive Plus

Revision	Datetime	Status	ChangeLog Entry
0	2020-11-12 01:56:26	ID requested
⏵ 1	2021-11-03 05:55:25	announced

Dataset with its publication pending

submitter keyword: N-glycosylation

glycoprotein

ER quality control mechanism

ER- associated degradation pathway

Xiaojuan Liu
contact affiliation	Institute of Marine Sciences, Guangdong Provincial Key Laboratory of Marine Biotechnology and STU-UNIVPM Joint Algal Research Center, College of Sciences, Shantou University, Shantou, Guangdong, China; Southern Marine Science and Engineering Guangdong Laboratory, Guangzhou, Guangdong, 515063, China.
contact email	liuxiaojuan@stu.edu.cn
lab head
Xiaojuan Liu
contact affiliation	Shantou University
contact email	liuxiaojuan@stu.edu.cn
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD022483
     1. Label: PRIDE project
     2. Name: Global profiling of N-glycosylated proteins in the diatom Phaeodactylum tricornutum