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Changing the phospholipid composition of Staphylococcus aureus causes distinct changes in membrane proteome and membrane‐sensory regulators
Author(s) -
Sievers Susanne,
M. Ernst Christoph,
Geiger Tobias,
Hecker Michael,
Wolz Christiane,
Becher Dörte,
Peschel Andreas
Publication year - 2010
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200900772
Subject(s) - proteome , proteomics , membrane protein , biology , cell envelope , phospholipid , lipidome , biochemistry , membrane fluidity , integral membrane protein , staphylococcus aureus , lipid bilayer , phosphatidylglycerol , membrane lipids , microbiology and biotechnology , membrane , bacteria , lipidomics , escherichia coli , genetics , phosphatidylcholine , gene
The dynamic lipid composition of bacterial cytoplasmic membranes has a profound impact on vital bacterial fitness and susceptibility to membrane‐damaging agents, temperature, or osmotic stress. However, it has remained largely unknown how changes in lipid patterns affect the abundance and expression of membrane proteins. Using recently developed gel‐free proteomics technology, we explored the membrane proteome of the important human pathogen Staphylococcus aureus in the presence or absence of the cationic phospholipid lysyl‐phosphatidylglycerol (Lys‐PG). We were able to detect almost half of all theoretical integral membrane proteins and could reliably quantify more than 35% of them. It is worth noting that the deletion of the Lys‐PG synthase MprF did not lead to a massive alteration but a very distinct up‐ or down‐regulation of only 1.5 or 3.5% of the quantified proteins. Lys‐PG deficiency had no major impact on the abundance of lipid‐biosynthetic enzymes but significantly affected the amounts of the cell envelope stress‐sensing regulatory proteins such as SaeS and MsrR, and of the SaeS‐regulated proteins Sbi, Efb, and SaeP. These data indicate very critical interactions of membrane‐sensory proteins with phospholipids and they demonstrate the power of membrane proteomics for the characterization of bacterial physiology and pathogenicity.