Journal
ENVIRONMENTAL MICROBIOLOGY
Volume 15, Issue 6, Pages 1661-1673Publisher
WILEY
DOI: 10.1111/1462-2920.12013
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Funding
- Centre National de la Recherche Scientifique
- Centre International de Recherche au Frontiere de la Chimie (FRC)
- ANR (Agence Nationale de Recherche) [ANR-08-BLAN-0309-02]
- Association Vaincre la Mucoviscidose
- Agence Nationale de la Recherche (ANR) [ANR-08-BLAN-0309] Funding Source: Agence Nationale de la Recherche (ANR)
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Pyoverdines are siderophores produced by fluorescent Pseudomonads to acquire iron. At least 60 different pyoverdines produced by diverse strains have been chemically characterized. They all consist of a dihydroquinoline-type chromophore linked to a peptide. These peptides are of various lengths and the sequences are strain specific. Pyoverdine biosynthesis in Pseudomonas aeruginosa and fluorescent Pseudomonads is a complex process involving at least 12 different proteins, starting in the cytoplasm and ending in the periplasm. The cellular localization of pyoverdine precursors was recently shown to be consistent with their biosynthetic enzymes. In the cytoplasm, pyoverdine appears to be assembled at the inner membrane and particularly at the old cell pole of the bacterium. Mature pyoverdine is uniformly distributed throughout the periplasm, like the periplasmic enzyme PvdQ. Secretion of pyoverdine involves a recently identified ATP-dependent efflux pump, PvdRT-OpmQ. This efflux system does not only secrete newly synthesized pyoverdine but also pyoverdine that already transported iron into the bacterial periplasm and any pyoverdine-metal complex other than ferri-pyoverdine present in the periplasm. This review considers how these new insights into pyoverdine biosynthesis and secretion contribute to our understanding of the role of pyoverdine in iron and metal homeostasis in fluorescent Pseudomonads.
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