Subcellular localization of the pyoverdine biogenesis machinery of Pseudomonas aeruginosa: a membrane-associated "siderosome".

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Imperi F,Visca P

doi

10.1016/j.febslet.2013.08.039

subject

Has Abstract

pub_date

2013-11-01 00:00:00

pages

3387-91

issue

21

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(13)00668-6

journal_volume

587

pub_type

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