RESUMEN
Acyl-homoserine lactone synthases make specific AHL quorum sensing signals to aid virulence in Gram-negative bacteria. Here, we use solution NMR spectroscopy to demonstrate that the carrier protein-enzyme interface accurately reveals substrate recognition mechanisms in two quorum signal synthases.
Asunto(s)
Proteínas Bacterianas , Proteínas Portadoras , Proteínas Portadoras/metabolismo , Proteínas Bacterianas/metabolismo , Bacterias Gramnegativas/metabolismo , Percepción de Quorum , Virulencia , Acil-Butirolactonas/química , Acil-Butirolactonas/metabolismoRESUMEN
Acyl carrier proteins (ACPs) are universally conserved proteins amongst different species and are involved in fatty acid synthesis. Bacteria utilize ACPs as acyl carriers and donors for the synthesis of products such as endotoxins or acyl homoserine lactones (AHLs), which are used in quorum sensing mechanisms. In this study, wehave expressed isotopically labeled holo-ACP from Burkholderia mallei in Escherichia coli to assign 100% of non-proline backbone amide (HN) resonances, 95.5% of aliphatic carbon resonances and 98.6% of aliphatic hydrogen sidechain resonances.