Dataset Information

Inner membrane proteome of E. coli Min mutant

ABSTRACT: 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.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Escherichia Coli

SUBMITTER: Yu-Ling Shih

LAB HEAD: Yu-Ling Shih

PROVIDER: PXD002548 | Pride | 2016-02-23

REPOSITORIES: Pride

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Quantitative Proteomics Analysis Reveals the Min System of Escherichia coli Modulates Reversible Protein Association with the Inner Membrane.

Lee Hsiao-Lin HL Chiang I-Chen IC Liang Suh-Yuen SY Lee Der-Yen DY Chang Geen-Dong GD Wang Kwan-Yu KY Lin Shu-Yu SY Shih Yu-Ling YL

Molecular & cellular proteomics : MCP 20160217 5

The Min system of Escherichia coli mediates placement of the division septum at the midcell. It oscillates from pole to pole to establish a concentration gradient of the division inhibition that is high at the poles but low at the midcell; the cell middle thereby becomes the most favorable site for division. Although Min oscillation is well studied from molecular and biophysical perspectives, it is still an enigma as to whether such a continuous, energy-consuming, and organized movement of the M ...[more]

PMID: 26889046

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			Action	DRS
	2014-0403_iTRAQ-1.msf	Msf
	2014-0403_iTRAQ-1.raw	Raw
	2014-0403_iTRAQ-2.msf	Msf
	2014-0403_iTRAQ-2.raw	Raw
	2014-0403_iTRAQ-3.msf	Msf