PXD023797

PXD023797 is an original dataset announced via ProteomeXchange.

Title	Escherichia coli S2P family intramembrane protease RseP is engaged in the regulated sequential cleavages of FecR in the ferric citrate signaling
Description	Escherichia coli RseP, a member of the S2P family intramembrane proteases, is involved in the activation of the σE extracytoplasmic stress response and the elimination of remnant signal peptides. It remains however unclear whether RseP has additional cellular functions. In this study, we attempted to identify new RseP substrates to explore still unknown physiological roles of this protease. Our mass spectrometry-based quantitative proteomic analysis revealed that the levels of the several Fec system proteins encoded by the fecABCDE operon (fec operon) were significantly decreased in an RseP-deficient strain. The Fec system is responsible for the uptake of ferric citrate, and the transcription of the fec operon is controlled by FecI, an alternative sigma factor, and its regulator FecR, a single-pass transmembrane protein. The assays with the fec operon expression reporter demonstrated that the proteolytic activity of RseP is essential for the ferric citrate-dependent up-regulation of the fec operon. Analysis using the FecR protein and FecR-derived model proteins showed that FecR undergoes sequential processing at the membrane and that RseP participates in the last step of this sequential processing to generate the N-terminal cytoplasmic fragment of FecR that acts in transcription of the fec operon with FecI. Ferric citrate signal-dependent generation of this cleavage product is the essential and sufficient role of RseP in the transcriptional activation of the fec operon. Our study unveiled a novel physiological role of E. coli RseP, intramembrane proteolysis of FecR, which is essential for the regulation of iron uptake by the ferric citrate transport system.
HostingRepository	jPOST
AnnounceDate	2021-04-14
AnnouncementXML	Submission_2022-09-18_02:31:54.389.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Tomoya Niinae
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	S-carboxamidomethyl-L-cysteine; L-methionine sulfoxide; TMT6plex reporter+balance reagent N-acylated residue; TMT6plex reporter+balance reagent acylated N-terminal
Instrument	instrument

Revision	Datetime	Status	ChangeLog Entry
0	2021-01-25 05:08:37	ID requested
1	2021-04-13 18:40:57	announced
2	2021-06-24 04:37:15	announced	2021-06-24: Updated PubMed.
⏵ 3	2022-09-18 02:31:55	announced	2022-09-18: Updated FTP location.

Yokoyama T, Niinae T, Tsumagari K, Imami K, Ishihama Y, Hizukuri Y, Akiyama Y, The Escherichia coli S2P intramembrane protease RseP regulates ferric citrate uptake by cleaving the sigma factor regulator FecR. J Biol Chem, 296():100673(2021) [pubmed]

submitter keyword: E.coli, membrane, TMT

Tatsuhiko Yokoyama
lab head
Tomoya Niinae
contact affiliation	Kyoto university
dataset submitter

jPOST dataset URI

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