PXD015985

PXD015985 is an original dataset announced via ProteomeXchange.

Title	Non-competitive binding of PpiD and YidC to the SecYEG translocon expands the global view on the SecYEG interactome in E. coli
Description	The SecYEG translocon constitutes the major protein transport channel in bacteria and transfers an enormous variety of different secretory and inner-membrane proteins. The minimal core of the SecYEG translocon consists of three inner-membrane proteins, SecY, SecE, and SecG, which, together with appropriate targeting factors, are sufficient for protein transport in vitro. However, in vivo the SecYEG translocon has been shown to associate with multiple partner proteins, likely allowing the SecYEG translocon to process its diverse substrates. To obtain a global view on SecYEG plasticity in Escherichia coli, here we performed a quantitative interaction proteomic analysis, which identified several known SecYEG-interacting proteins, verified the interaction of SecYEG with quality-control proteins, and revealed several previously unknown putative SecYEG interacting proteins. Surprisingly, we found that the chaperone complex PpiD/YfgM is the most prominent interaction partner of SecYEG. Detailed analyses of the PpiD–SecY interaction by site-directed cross-linking revealed that PpiD and the established SecY partner protein YidC use almost completely overlapping binding sites on SecY. Both PpiD and YidC contacted the lateral gate, the plug domain, and the periplasmic cavity of SecY. However, quantitative MS and cross-linking analyses revealed that despite having almost identical binding sites, their binding to SecY is non-competitive. This observation suggests that the SecYEG translocon forms different substrate-independent subassemblies in which SecYEG either associates with YidC or with the PpiD/YfgM complex. In summary, the results of this study indicate that the PpiD/YfgM chaperone complex is a primary interaction partner of the SecYEG translocon.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_03:59:19.063.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Friedel Drepper
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2019-10-23 05:49:34	ID requested
1	2019-11-07 06:31:30	announced
2	2019-11-12 23:34:00	announced	2019-11-13: Updated publication reference for PubMed record(s): 31699901.
3	2019-11-27 06:51:41	announced	2019-11-27: Updated project metadata.
⏵ 4	2024-10-22 03:59:27	announced	2024-10-22: Updated project metadata.

10.1074/jbc.ra119.010686;

Jauss B, Petriman NA, Drepper F, Franz L, Sachelaru I, Welte T, Steinberg R, Warscheid B, Koch HG, . J Biol Chem, 294(50):19167-19183(2019) [pubmed]

curator keyword: Biological

submitter keyword: interaction proteomics, YidC, PpiD, protein translocation,SecYEG translocon, protein cross-linking, protein-protein interaction, quantitative affinity purification mass spectrometry (qAP-MS)

Bettina Warscheid
contact affiliation	Functional Proteomics Lab, Faculty of Biology, University of Freiburg, Germany
contact email	bettina.warscheid@biologie.uni-freiburg.de
lab head
Friedel Drepper
contact affiliation	AG Warscheid Biologie II Albert-Ludwigs-Universität Freiburg Schänzlestr. 1 79104 Freiburg Germany
contact email	friedel.drepper@biologie.uni-freiburg.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD015985
     1. Label: PRIDE project
     2. Name: Non-competitive binding of PpiD and YidC to the SecYEG translocon expands the global view on the SecYEG interactome in E. coli