Quantitative Proteomics Analysis Reveals the Min System of Escherichia coli Modulates Reversible Protein Association
Hsiao-Lin Lee1, I-Chen Chiang1, Suh-Yuen Liang1
1From the ‡Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan;
Abstract:
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 Min proteins would affect cellular processes other than the division site selection. To tackle this question, we compared the inner membrane proteome of the wild-type and Δmin strains using a quantitative approach. Forty proteins that showed differential abundance on the inner membrane of the mutant cells were identified and defined as proteins of interest (POIs). More than half of the POIs were peripheral membrane proteins, suggesting that the Min system affects mainly reversible protein association with the inner membrane. In addition, 6 out of 10 selected POIs directly interacted with at least one of the Min proteins, confirming the correlation between POIs and the Min system.Further analysis revealed a functional relationship between metabolism and the Min system. Metabolic enzymes accounted for 45% of the POIs, and there was a change of metabolites in the related reactions. We hypothesize that the Min system could alter the membrane location of proteins to modulate their enzymatic activity. Thus, the metabolic modulation in the Δmin mutant is likely an adaptive phenotype in cells of abnormal size and chromosome number due to an imbalanced abundance of proteins on the inner membrane. Taken together, the current work reports novel interactions of the Min system and reveals a global physiological impact of the Min system in addition to the division site placement.
Insights
The Min system in E. coli regulates cell division. This study reveals it also impacts cell metabolism by altering protein associations with the inner membrane.
Area of Science:
- Microbiology
- Cell Biology
- Biochemistry
Background:
- The Min system in Escherichia coli is crucial for accurate cell division by establishing a gradient that directs septum formation to the midcell.
- Min protein oscillation is well-characterized molecularly and biophysically, but its broader cellular roles remain unclear.
Purpose of the Study:
- To investigate potential cellular processes affected by the Min system beyond division site selection.
- To identify proteins whose abundance or localization is altered by the Min system.
Main Methods:
- Quantitative proteomic analysis of the inner membrane proteome comparing wild-type and Δmin mutant Escherichia coli strains.
- Identification and characterization of differentially abundant proteins (proteins of interest, POIs).
- Analysis of interactions between POIs and Min proteins, and their functional enrichment in metabolic pathways.
Main Results:
- Forty proteins of interest (POIs) were identified with differential abundance in the Δmin mutant's inner membrane.
- Over half of the POIs were peripheral membrane proteins, indicating the Min system influences reversible protein-membrane associations.
- Metabolic enzymes constituted 45% of POIs, with associated metabolite changes, suggesting a link between the Min system and cellular metabolism.
Conclusions:
- The Min system influences protein localization at the inner membrane, impacting cellular processes beyond division site placement.
- A functional link between the Min system and cellular metabolism is revealed, potentially through modulation of metabolic enzyme activity.
- Metabolic alterations in Δmin mutants may represent adaptive responses to aberrant cell morphology and chromosome number caused by altered inner membrane protein composition.
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