PXD003098

PXD003098 is an original dataset announced via ProteomeXchange.

Title	In vivo trapping of thioredoxin substrates
Description	Thioredoxin (Trx) is a ubiquitous oxidoreductase maintaining protein-bound cysteine residues in the reduced thiol state. Here, we combined a well-established method to trap Trx substrates with the power of bacterial genetics to comprehensively characterize the in vivo Trx redox interactome in the model bacterium Escherichia coli. Using strains engineered to optimize trapping, we report the identification of a total 257 Trx substrates, including 191 that had never been reported to depend on Trx for reduction. The newly identified Trx substrates are involved in a variety of cellular processes, ranging from energy metabolism to amino acid synthesis and transcription. The interaction between Trx and two of its newly identified substrates, a protein required for the import of most carbohydrates, PtsI, and the bacterial actin homolog MreB was studied in detail. We provide direct evidence that PtsI and MreB contain cysteine residues that are susceptible to oxidation and that participate in the formation of an intermolecular disulfide with Trx. By considerably expanding the number of Trx targets, our work highlights the role played by this major oxidoreductase in a variety of cellular processes. Moreover, as the dependence on Trx for reduction is often conserved across species, it also provides insightful information on the interactome of Trx in organisms other than E. coli
HostingRepository	PRIDE
AnnounceDate	2016-04-19
AnnouncementXML	Submission_2016-04-19_09:59:49.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Didier Vertommen
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	LTQ

Revision	Datetime	Status	ChangeLog Entry
0	2015-10-22 02:50:24	ID requested
⏵ 1	2016-04-19 09:59:50	announced

Arts IS, Vertommen D, Baldin F, Laloux G, Collet JF, Comprehensively Characterizing the Thioredoxin Interactome In Vivo Highlights the Central Role Played by This Ubiquitous Oxidoreductase in Redox Control. Mol Cell Proteomics, 15(6):2125-40(2016) [pubmed]

submitter keyword: TRX1, substrates, E. Coli

Jean-François Collet
contact affiliation	UCL - de Duve Institute - Brussels Center for Redox Biology, 1200 Brussels Belgium
contact email	jfcollet@uclouvain.be
lab head
Didier Vertommen
contact affiliation	UCL - de Duve Institute, Brussels Belgium
contact email	didier.vertommen@uclouvain.be
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD003098
     1. Label: PRIDE project
     2. Name: In vivo trapping of thioredoxin substrates