PXD003766

PXD003766 is an original dataset announced via ProteomeXchange.

Title	Proteolytic-independent role of mycosins in stabilization of the ESX-1 and ESX-5 type VII secretion membrane complexes.
Description	Pathogenic mycobacteria contain up to five type VII secretion (T7S) systems, ESX-1 to ESX-5, which have central roles in virulence and viability. One of the conserved components of these systems, the serine protease mycosin (MycP), has been shown to be essential for secretion by ESX-1 and ESX-5. However, here we show that protease activity of MycP1 and MycP5 of M. marinum is not essential for ESX-1 and ESX-5 dependent secretion, respectively. This indicates that MycP has a second, so far unknown, function that is essential for T7S. To investigate whether this second role is related to proper functioning of the T7S membrane core complex, we first verified that the ESX-1 membrane complex is of similar composition and size as the previously analyzed ESX-5 complex and that MycP1 and MycP5 are not an integral part of the respective core complex. In contrast, we could not detect ESX-1 and ESX-5 complexes under mycP1 and mycP5 knockout conditions, respectively. Interestingly, the ESX-5 complex could be detected at wild-type levels in the absence of MycP5, when membranes were subjected to crosslinking before detergent solubilization, suggesting that MycP is involved in complex stabilization. Based on our findings we hypothesize that mycosins loosely associate with their respective membrane complex, which is crucial for the full integrity and functioning of the secretion machinery.
HostingRepository	PRIDE
AnnounceDate	2016-10-11
AnnouncementXML	Submission_2019-02-12_08:06:04.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Sander Piersma
SpeciesList	scientific name: Mycobacterium marinum ATCC BAA-535; NCBI TaxID: 1348799;
ModificationList	monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2016-03-10 06:54:11	ID requested
1	2016-10-11 04:09:10	announced
⏵ 2	2019-02-12 08:06:06	announced	Updated publication reference for PubMed record(s): 27795391.

van Winden VJ, Ummels R, Piersma SR, Jim, é, nez CR, Korotkov KV, Bitter W, Houben EN, Mycosins Are Required for the Stabilization of the ESX-1 and ESX-5 Type VII Secretion Membrane Complexes. mBio, 7(5):(2016) [pubmed]

curator keyword: Biological, Biomedical

submitter keyword: Mycobacterium marinum, tuberculosis, ESX1, ESX5, T7S, label-free, single-shot

Connie Ramona Jimenez
contact affiliation	OncoProteomics Laboratory, Dept of Medical Oncology, VU University Medical Center, Amsterdam, The Netherlands
contact email	c.jimenez@vumc.nl
lab head
Sander Piersma
contact affiliation	OncoProteomics Laboratory, dept of Medical Oncology, VUmc Medical Center, Amsterdam, The Netherlands
contact email	s.piersma@vumc.nl
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/2016/10/PXD003766

PRIDE project URI

• PRIDE
  1. PXD003766
     1. Label: PRIDE project
     2. Name: Proteolytic-independent role of mycosins in stabilization of the ESX-1 and ESX-5 type VII secretion membrane complexes.