Identification of the fatty acid coenzyme-A ligase FadD1 as an interacting partner of FptX in the Pseudomonasaeruginosa pyochelin pathway.

Abstract

Pseudomonasaeruginosa is one of the most important nosocomial bacteria emerging as a highly multidrug-resistant pathogen. P.aeruginosa produces two siderophores including pyochelin (PCH) to fulfil its need for iron during infections. We know that both outer and inner membrane proteins FptA and FptX are involved in the ferri-PCH uptake, but this process requires increasing molecular and biochemical knowledge. Here, using bacterial two-hybrid and copurification assays we identified the fatty acid coenzyme-A ligase FadD1 as a novel interacting partner of the inner membrane transporter FptX and found that FadD1 may play a role in PCH production. We managed to purify the FadD1-FptX inner membrane complex and obtained low-resolution 3D models, opening the way for future high-resolution structures.