PXD039132

PXD039132 is an original dataset announced via ProteomeXchange.

Title	Large-scale qualitative and quantitative research of dityrosine crosslinking omics in Escherichia coli
Description	Excessive reactive oxygen species cause oxidative stress in cells. Two molecules of tyrosine can generate dityrosine, which is not only a product of natural posttranslational processes, but also a putative biomarker for protein oxidation. Few studies have investigated dityrosine crosslinking under endogenous or exogenous oxidative conditions in Escherichia coli at the proteome level so far. In this study, in order to investigate qualitative and quantitative dityrosine crosslinking, two mutant strains were constructed as endogenous oxidative stress model, as well as one mutant strain added with 1mM H2O2 as exogenous oxidative stress model. We integrated label-free LC-MS/MS and bioinformatics to research dityrosine crosslinking in Escherichia coli. A large-scale dataset of dityrosine crosslinking was provided. 352 proteins were identified to participate in dityrosine crosslinking by pLink. The subcellular localization included cytoplasmic (61.93%), periplasmic (21.31%), outer membrane (7.95%), inner membrane (5.97%) and extracellular (2.84%). Quantitative analysis of dityrosine crosslinking indicated that the three oxidative stress models could be separated at dityrosine linked peptides level. We expect that our research will guide efforts to comprehend the detailed features of dityrosine crosslinking in future.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_08:47:24.248.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Zhou Xiangzhe
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	iodoacetamide derivatized residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2023-01-02 01:20:19	ID requested
1	2023-05-10 14:23:37	announced
⏵ 2	2023-11-14 08:47:25	announced	2023-11-14: Updated project metadata.

Zhou X, Liu F, Li N, Zhang Y, . Antioxidants (Basel), 12(4):(2023) [pubmed]

submitter keyword: Hydrogen peroxide,Dityrosine crosslinking, Label-free proteomics

Yongqian Zhang
contact affiliation	School of Life Science, Beijing Institute of Technology
contact email	zyq@bit.edu.cn
lab head
Zhou Xiangzhe
contact affiliation	Beijing Institute of Technology
contact email	3120211440@bit.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/PXD039132

PRIDE project URI

• PRIDE
  1. PXD039132
     1. Label: PRIDE project
     2. Name: Large-scale qualitative and quantitative research of dityrosine crosslinking omics in Escherichia coli