PXD002548

PXD002548 is an original dataset announced via ProteomeXchange.

Title	Inner membrane proteome of E. coli Min mutant
Description	In bacteria, proteins of the MinD/ParA superfamily are reported to partition DNA and protein complexes to designate subcellular location. Among them, the E. coli Min system is a prominent example to demonstrate that the protein function is spatially regulated by the dynamic subcellular localization and by the reversible membrane topology. It is curious that pole-to-pole oscillation of MinDE involves continuous cycles of protein attachment to and detachment from the membrane, an environment that is crowded with a variety of proteins of different functions. We therefore took a quantitative proteomic approach, the isobaric tags for relative and absolute quantitation (iTRAQ) method, to analyze the inner memrbane proteome of the wild-type and Min mutant strains, aiming at identifying membrane and memrbane associated proteins that are affected in the absence of the Min system. The study reveals a physiological adapation strategy that could be used to rescue the unproductive rounds of cell division. The study also suggests that partition of macromolecules by the MinD/ParA family of proteins may have broader roles in bacterial physiology.
HostingRepository	PRIDE
AnnounceDate	2016-02-23
AnnouncementXML	Submission_2016-02-23_03:05:23.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Yu-Ling Shih
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	LTQ Orbitrap Elite

Revision	Datetime	Status	ChangeLog Entry
0	2015-07-16 03:26:40	ID requested
⏵ 1	2016-02-23 03:05:24	announced

Lee HL, Chiang IC, Liang SY, Lee DY, Chang GD, Wang KY, Lin SY, Shih YL, Quantitative Proteomics Analysis Reveals the Min System of Escherichia coli Modulates Reversible Protein Association with the Inner Membrane. Mol Cell Proteomics, 15(5):1572-83(2016) [pubmed]

submitter keyword: E. coli, cell division, the Min system, iTRAQ, membrane

Yu-Ling Shih
contact affiliation	Institute of Biological Chemistry, Academia Sinica, Taiwan
contact email	ylshih10@gate.sinica.edu.tw
lab head
Yu-Ling Shih
contact affiliation	Academia Sinica
contact email	ylshih10@gate.sinica.edu.tw
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD002548
     1. Label: PRIDE project
     2. Name: Inner membrane proteome of E. coli Min mutant