PXD005597

PXD005597 is an original dataset announced via ProteomeXchange.

Title	FliP subcomplex analysis
Description	Biosynthesis of the bacterial flagellum depends on a flagellar-specific type III secretion system (T3SS), a protein export machine homologous to the export machinery of the virulence-associated injectisome. Six cytoplasmic (FliH/I/J/G/M/N) and seven integral membrane proteins (FlhA/B FliF/O/P/Q/R) form the flagellar basal body and are involved in transport of flagellar building blocks across the inner membrane in a protein motive force-dependent manner. FlhA/B and FliP/Q/R are conserved in all T3SS and form the export gate complex. FliO is absent in some T3SS and was presumed to regulate FliP during flagellum assembly. However, the molecular function of FliO and how the large, multi-component transmembrane export gate complex assembles in a coordinated manner remained enigmatic. Here, we demonstrate that FliO protects FliP from proteolytic degradation and promotes formation of FliP-containing subcomplexes during the first step of core export apparatus assembly. We further reveal the sub-cellular localization of FliO by dSTORM superresolution microscopy and show that FliO is not part of the assembled flagellar basal body. In summary, our results suggest that FliO functions as a novel, flagellar T3SS-specific chaperone, which facilitates quality control and productive assembly of the core T3SS export machinery.
HostingRepository	PRIDE
AnnounceDate	2017-08-22
AnnouncementXML	Submission_2017-08-22_05:44:09.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Nicolas Nalpas
SpeciesList	scientific name: Salmonella enterica subsp. enterica serovar Typhimurium; NCBI TaxID: 90371;
ModificationList	monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	LTQ Orbitrap

Revision	Datetime	Status	ChangeLog Entry
0	2016-12-20 00:33:14	ID requested
⏵ 1	2017-08-22 05:44:11	announced

Fabiani FD, Renault TT, Peters B, Dietsche T, G, á, lvez EJC, Guse A, Freier K, Charpentier E, Strowig T, Franz-Wachtel M, Macek B, Wagner S, Hensel M, Erhardt M, A flagellum-specific chaperone facilitates assembly of the core type III export apparatus of the bacterial flagellum. PLoS Biol, 15(8):e2002267(2017) [pubmed]

curator keyword: Biological, Biomedical

submitter keyword: T3SS, FliP, FliO, export gate complex, assembly

Marc Erhardt
contact affiliation	Junior Research Group Infection Biology of Salmonella Helmholtz Centre for Infection Research Inhoffenstraße 7 38124 Braunschweig Germany
contact email	marc.erhardt@helmholtz-hzi.de
lab head
Nicolas Nalpas
contact affiliation	Tuebingen University
contact email	nalpas.nicolas@gmail.com
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/2017/08/PXD005597

PRIDE project URI

• PRIDE
  1. PXD005597
     1. Label: PRIDE project
     2. Name: FliP subcomplex analysis