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Subcellular localization of the pyoverdine biogenesis machinery of Pseudomonas aeruginosa : A membrane‐associated “siderosome”
Author(s) -
Imperi Francesco,
Visca Paolo
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.08.039
Subject(s) - pyoverdine , siderophore , pseudomonas aeruginosa , biogenesis , nonribosomal peptide , biology , bacterial outer membrane , biochemistry , cytoplasm , microbiology and biotechnology , enzyme , glyoxylate cycle , bacteria , biosynthesis , gene , escherichia coli , genetics
The peptidic siderophore pyoverdine is the primary iron uptake system of fluorescent pseudomonads, and a virulence factor in the opportunistic pathogen Pseudomonas aeruginosa . Pyoverdine biogenesis is a co‐ordinate process requiring several precursor‐generating enzymes and large nonribosomal peptide synthetases (NRPSs) in the cytoplasm, followed by extracytoplasmic maturation. By using cell fractionation, protein–protein interaction, and in vivo labeling assays we obtained evidence that, in P. aeruginosa , pyoverdine NRPSs assemble with precursor‐generating enzymes into a membrane‐bound multi‐enzymatic complex, for which we propose the name “siderosome”. The pyoverdine biogenetic complex represents a novel example of subcellular compartmentalization of a secondary metabolic pathway in prokaryotes.