A Conserved Hydrolase Responsible for the Cleavage of Aminoacylphosphatidylglycerol in the Membrane of Enterococcus faecium
Abbreviated Journal Title
J. Biol. Chem.
RHIZOBIUM-TROPICI CIAT899; VIRULENCE GENE ACVB; STAPHYLOCOCCUS-AUREUS; LYSYL-PHOSPHATIDYLGLYCEROL; AGROBACTERIUM-TUMEFACIENS; ANTIMICROBIAL; PEPTIDES; IV SECRETION; RESISTANCE; PROTEIN; DAPTOMYCIN; Biochemistry & Molecular Biology
Aminoacylphosphatidylglycerol synthases (aaPGSs) are enzymes that transfer amino acids from aminoacyl-tRNAs (aa-tRNAs) to phosphatidylglycerol (PG) to form aa-PG in the cytoplasmic membrane of bacteria. aa-PGs provide bacteria with resistance to a range of antimicrobial compounds and stress conditions. Enterococcus faecium encodes a triple-specific aaPGS (RakPGS) that utilizes arginine, alanine, and lysine as substrates. Here we identify a novel hydrolase (AhyD), encoded immediately adjacent to rakPGS in E. faecium, which is responsible for the hydrolysis of aa-PG. The genetic synteny of aaPGS and ahyD is conserved in >60 different bacterial species. Deletion of ahyD in E. faecium resulted in increased formation of Ala-PG and Lys-PG and increased sensitivity to bacitracin. Our results suggest that AhyD and RakPGS act together to maintain optimal levels of aa-PG in the bacterial membrane to confer resistance to certain antimicrobial compounds and stress conditions.
Journal of Biological Chemistry
"A Conserved Hydrolase Responsible for the Cleavage of Aminoacylphosphatidylglycerol in the Membrane of Enterococcus faecium" (2013). Faculty Bibliography 2010s. 2571.