Authors

A. M. Smith; J. S. Harrison; K. M. Sprague;H. Roy

Comments

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Abbreviated Journal Title

J. Biol. Chem.

Keywords

RHIZOBIUM-TROPICI CIAT899; VIRULENCE GENE ACVB; STAPHYLOCOCCUS-AUREUS; LYSYL-PHOSPHATIDYLGLYCEROL; AGROBACTERIUM-TUMEFACIENS; ANTIMICROBIAL; PEPTIDES; IV SECRETION; RESISTANCE; PROTEIN; DAPTOMYCIN; Biochemistry & Molecular Biology

Abstract

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 Title

Journal of Biological Chemistry

Volume

288

Issue/Number

31

Publication Date

1-1-2013

Document Type

Article

Language

English

First Page

22768

Last Page

22776

WOS Identifier

WOS:000330596300054

ISSN

0021-9258

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