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Investigating the Role of the Escherichia coli Lysophospholipase PldB in Determining Cell Length
Author(s) -
Nikpour Naveed,
Garrett Teresa A
Publication year - 2019
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.2019.33.1_supplement.796.11
Subject(s) - cell , phosphatidylglycerol , lysophospholipase , glycerophospholipid , cell membrane , escherichia coli , biochemistry , microbiology and biotechnology , cell division , chemistry , membrane , biology , phospholipid , phosphatidylcholine , gene , enzyme , phospholipase
Headgroup acylated glycerophospholipids (GPLs) are proposed to carry out an essential function in cell division in the cell membranes of Escherichia coli . Lysophospholipase L 2 (PldB) has been shown to transfer the acyl group from 2‐acyl‐lysophospholipids to the headgroup of phosphatidylglycerol (PG) to form acyl PG. Cells overexpressing PldB have been found to show an elongated cell phenotype. As the cause for this phenotype is not entirely known, we aim to develop a robust assay to test PldB activity so as to understand what aspect of PldB activity is implicated in the cell elongation phenotype. We are developing a radiochemical thin‐layer chromatography assay for PldB using 14 C PG and 14 C ( bis ‐monoacylglycerol)phosphate to the study this mechanism. Using liquid chromatography‐mass spectrometry‐based assays, we are testing cells with mutations to PldB's catalytic triad to determine a catalytically dead mutant. This mutant would allow us to assess if cell elongation requires PldB activity or if PldB's association with the inner membrane impacts the activity of cellular division machinery. This project aims to undercover more information about the functioning of PldB and headgroup acylated GPLs. Due to PldB's role in cell membrane integrity, further analysis of its mechanism may further our understanding of how the cell membrane functions during cell division. Future research can focus on localizing PldB within the membrane to help assess PldB's function during cell division. Support or Funding Information This work was funded by National Science Foundation Research at Undergraduate Institution Award #1516805 to T. A. G. This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .