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The PhoP/PhoQ two‐component regulatory system influences on Escherichia coli headgroup‐acylated glycerophospholipids
Author(s) -
DiNardo Acadia S.,
Garrett Teresa A.
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.539.19
Subject(s) - glycerophospholipids , phosphatidylglycerol , escherichia coli , chemistry , biochemistry , bacteria , peptide , phospholipid , biology , membrane , gene , genetics , phosphatidylcholine
Headgroup‐acylated glycerophospholipids (GPLs) are a class of low abundance membrane lipids that are thought to play a roll in cell division and membrane integrity in Gram‐negative bacteria, such as Escherichia coli . The PhoP/PhoQ two‐component regulatory system is known to aid in virulence of pathogenic E. coli and responds to low Mg 2+ concentrations. Previous research has suggested a protein activated by the PhoP/PhoQ system increases synthesis of acyl phosphatidylglycerol (acyl PG), a type of headgroup‐acylated GPL. Currently, though, the synthase of another headgroup‐acylated GPL, N ‐acyl phosphatidylethanolamines ( N ‐acyl PE), is unknown. In order to determine if the PhoP/PhoQ system affects levels of acyl PGs, as well as N ‐acyl PEs, wild‐type MG1655 E. coli with an empty pBAD 33.1 plasmid were grown in N‐minimal media with Mg 2+ concentrations of either 8μM or 10mM. To confirm the activation of the PhoP/PhoQ system when cells are grown in 8μM Mg2+ media a reporter strain of E. coli, pNL3, was used. A β‐galactosidase assay of the pNL3 stain confirmed the activation of the PhoP/PhoQ system in low Mg 2+ conditions through a 3.8 fold increase of activity in 8μM Mg 2+ conditions compared to growths in 10mM Mg 2+ . In the MG1655 wild‐type strain, three normalized N ‐acyl PE and four normalized acyl PG species were measured, utilizing reverse phase column mass spectrometry, and summed in each Mg 2+ condition. N ‐acyl PE and acyl PG levels in the 8μM Mg 2+ growth was double that of the MG1655 grown in 10mM Mg 2+ . These data suggest that the PhoP/PhoQ system may be implicated in the synthesis of N ‐acyl PEs and acyl PGs. Further research is required to verify the correlation between the activated PhoP/PhoQ system in N ‐acyl PE and acyl PG synthase, as well as identify the protein specifically responsible for the synthesis of N ‐acyl PEs. Support or Funding Information Supported by National Science Foundation Major Research Instrumentation grant #1039659 and Research at Undergraduate Institution grant #1516805. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .