PXD029340

PXD029340 is an original dataset announced via ProteomeXchange.

Title	Insight into the interplay between thiol oxidoreductases of oxidative activity of Campylobacter jejuni
Description	The bacterial proteins of the Dsb family catalyze the formation of disulfide bridges between cysteine residues that stabilize protein structures and ensure their proper functioning. Here we report the detailed analysis of the Dsb pathway of Campylobacter jejuni. The oxidizing Dsb system of this pathogen is unique because it consists of two monomeric DsbAs (DsbA1 and DsbA2) and one dimeric bifunctional protein (C8J_1298). Previously, we showed that DsbA1 and C8J_1298 are redundant. Here we unraveled the interaction between the two monomeric DsbAs by in vitro and in vivo experiments and by solving their structures and found that both monomeric DsbAs are dispensable proteins. Their structures confirmed that they are homologs of EcDsbL. The slight differences seen in the surface charge of the proteins do not affect the interaction with their redox partner. Comparative proteomics showed that several respiratory proteins, as well as periplasmic transport proteins, are targets of the Dsb system. Some of these, both donors and electron acceptors, are essential elements of C. jejuni respiratory process under oxygen-limiting conditions in the host intestine. The data presented provides detailed information on function of the C. jejuni Dsb system, identifying it as a potential target for novel antibacterial molecules.
HostingRepository	PRIDE
AnnounceDate	2022-02-22
AnnouncementXML	Submission_2022-02-22_04:23:24.766.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD029340
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Agata Malinowska
SpeciesList	scientific name: Campylobacter jejuni subsp. jejuni 81116; NCBI TaxID: 407148;
ModificationList	methylthiolated residue; monohydroxylated residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2021-10-25 06:44:31	ID requested
⏵ 1	2022-02-22 04:23:26	announced

Bana, ś AM, Bocian-Ostrzycka KM, Dunin-Horkawicz S, Ludwiczak J, Wilk P, Orlikowska M, Wyszy, ń, ska A, D, ą, browska M, Plichta M, Spodzieja M, Pola, ń, ska MA, Malinowska A, Jagusztyn-Krynicka EK, and Their Impact on Bacterial Physiology and Pathogenesis. Int J Mol Sci, 22(24):(2021) [pubmed]

submitter keyword: Dsb, Campylobacter, bacteria

Katarzyna Jagusztyn-Krynicka
contact affiliation	Department of Bacterial Genetics, Institute of Microbiology, Faculty of Biology, University of Warsaw, Poland
contact email	kjkryn@gmail.com
lab head
Agata Malinowska
contact affiliation	IBB PAS
contact email	esme@ibb.waw.pl
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/2022/02/PXD029340

PRIDE project URI

• PRIDE
  1. PXD029340
     1. Label: PRIDE project
     2. Name: Insight into the interplay between thiol oxidoreductases of oxidative activity of Campylobacter jejuni