RRC ID 55829
Author Jeucken A, Helms JB, Brouwers JF.
Title Cardiolipin synthases of Escherichia coli have phospholipid class specific phospholipase D activity dependent on endogenous and foreign phospholipids.
Journal Biochim Biophys Acta Mol Cell Biol Lipids
Abstract E. coli has three Cls-isoenzymes for cardiolipin (CL) synthesis but the differences between these three enzymes remain unresolved. All three Cls enzymes contain the phospholipase D (PLD) characteristic HKD motive and synthesize CL using PLD activity. Here, using LC-MS we show the effect of overexpressing or deletion of the three individual Cls enzymes on the lipidome, which included changes in lipid class distribution and CL species profiles. We demonstrate, for the first time, that overexpression of only ClsB resulted in the appreciable synthesis of a variety of phosphatidylalcohols, thereby establishing a 'classic' PLD activity for this enzyme: phospholipid headgroup exchange. Endogenous E. coli lipids and primary alcohols were substrates for this trans-phosphatidylation reaction. Furthermore, we show that endogenous levels of ClsA mediated a similar trans-phosphatidylation reaction to form phosphatidylalcohols, however this reaction was dependent on the presence of the foreign phospholipid class phosphatidylcholine (PC). This allows us to clarify the different specificities of the cardiolipin synthases.
Volume 1863(10)
Pages 1345-1353
Published 2018-10-1
DOI 10.1016/j.bbalip.2018.06.017
PII S1388-1981(18)30140-9
PMID 29933046
MeSH Alcohols / metabolism Chromatography, Liquid Escherichia coli / enzymology* Escherichia coli Proteins / genetics Escherichia coli Proteins / metabolism Gene Deletion Membrane Proteins / genetics Membrane Proteins / metabolism* Multigene Family Phosphatidylcholines / metabolism Phospholipase D / metabolism* Phospholipids / metabolism* Substrate Specificity Tandem Mass Spectrometry Transferases (Other Substituted Phosphate Groups) / genetics Transferases (Other Substituted Phosphate Groups) / metabolism*
IF 4.402
Times Cited 9
Resource
Prokaryotes E. coli ASKA(-) collection, ME5305, BW25113, Keio collection