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- W2890948890 endingPage "17996" @default.
- W2890948890 startingPage "17985" @default.
- W2890948890 abstract "Modifications to the Gram-positive bacterial cell wall play important roles in antibiotic resistance and pathogenesis, but the pathway for the d-alanylation of teichoic acids (DLT pathway), a ubiquitous modification, is poorly understood. The d-alanylation machinery includes two membrane proteins of unclear function, DltB and DltD, which are somehow involved in transfer of d-alanine from a carrier protein inside the cell to teichoic acids on the cell surface. Here, we probed the role of DltD in the human pathogen Staphylococcus aureus using both cell-based and biochemical assays. We first exploited a known synthetic lethal interaction to establish the essentiality of each gene in the DLT pathway for d-alanylation of lipoteichoic acid (LTA) and confirmed this by directly detecting radiolabeled d-Ala-LTA both in cells and in vesicles prepared from mutant strains of S. aureus We developed a partial reconstitution of the pathway by using cell-derived vesicles containing DltB, but no other components of the d-alanylation pathway, and showed that d-alanylation of previously formed lipoteichoic acid in the DltB vesicles requires the presence of purified and reconstituted DltA, DltC, and DltD, but not of the LTA synthase LtaS. Finally, based on the activity of DltD mutants in cells and in our reconstituted system, we determined that Ser-70 and His-361 are essential for d-alanylation activity, and we propose that DltD uses a catalytic dyad to transfer d-alanine to LTA. In summary, we have developed a suite of assays for investigating the bacterial DLT pathway and uncovered a role for DltD in LTA d-alanylation." @default.
- W2890948890 created "2018-09-27" @default.
- W2890948890 creator A5002399707 @default.
- W2890948890 creator A5020489268 @default.
- W2890948890 creator A5030692613 @default.
- W2890948890 creator A5057251906 @default.
- W2890948890 creator A5061764222 @default.
- W2890948890 date "2018-11-01" @default.
- W2890948890 modified "2023-10-14" @default.
- W2890948890 title "A partial reconstitution implicates DltD in catalyzing lipoteichoic acid d-alanylation" @default.
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- W2890948890 doi "https://doi.org/10.1074/jbc.ra118.004561" @default.
- W2890948890 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6240853" @default.
- W2890948890 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30237166" @default.