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
Smith, Angela M.; Harrison, Jesse S.; Sprague, Kevin M.; and Roy, Hervé, "A Conserved Hydrolase Responsible for the Cleavage of Aminoacylphosphatidylglycerol in the Membrane of Enterococcus faecium" (2013). Faculty Bibliography 2010s. 2571.