scholarly journals The feoB ferrous iron uptake pathway contributes to the intracellular survival of F. tularensis LVS

2012 ◽  
Vol 26 (S1) ◽  
Author(s):  
Cindy Arisa Thomas-Charles ◽  
Huaixin Zheng
Keyword(s):  
Ferrous Iron ◽  
Iron Uptake ◽  
Intracellular Survival ◽  
Uptake Pathway

scholarly journals Pyoverdine-Mediated Iron Uptake in Pseudomonas aeruginosa: the Tat System Is Required for PvdN but Not for FpvA Transport

2006 ◽  
Vol 188 (9) ◽  
pp. 3317-3323 ◽  
Author(s):  
Romé Voulhoux ◽  
Alain Filloux ◽  
Isabelle J. Schalk
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Outer Membrane ◽  
Iron Uptake ◽  
Cytoplasmic Membrane ◽  
Signal Sequence ◽  
Iron Release ◽  
Outer Membrane Receptor ◽  
Uptake Pathway ◽  
Uptake Process ◽  
Tat System

ABSTRACT Under iron-limiting conditions, Pseudomonas aeruginosa PAO1 secretes a fluorescent siderophore called pyoverdine (Pvd). After chelating iron, this ferric siderophore is transported back into the cells via the outer membrane receptor FpvA. The Pvd-dependent iron uptake pathway requires several essential genes involved in both the synthesis of Pvd and the uptake of ferric Pvd inside the cell. A previous study describing the global phenotype of a tat-deficient P. aeruginosa strain showed that the defect in Pvd-mediated iron uptake was due to the Tat-dependent export of proteins involved in Pvd biogenesis and ferric Pvd uptake (U. Ochsner, A. Snyder, A. I. Vasil, and M. L. Vasil, Proc. Natl. Acad. Sci. USA 99:8312-8317, 2002). Using biochemical and biophysical tools, we showed that despite its predicted Tat signal sequence, FpvA is correctly located in the outer membrane of a tat mutant and is fully functional for all steps of the iron uptake process (ferric Pvd uptake and recycling of Pvd on FpvA after iron release). However, in the tat mutant, no Pvd was produced. This suggested that a key element in the Pvd biogenesis pathway must be exported to the periplasm by the Tat pathway. We located PvdN, a still unknown but essential component in Pvd biogenesis, at the periplasmic side of the cytoplasmic membrane and showed that its export is Tat dependent. Our results further support the idea that a critical step of the Pvd biogenesis pathway involving PvdN occurs at the periplasmic side of the cytoplasmic membrane.

Ferrous iron uptake by Bifidobacterium bifidum var. Pennsylvanicus: The effect of metals and metabolic inhibitors

1987 ◽  
Vol 19 (6) ◽  
pp. 517-522 ◽  
Author(s):  
Anatoly Bezkorovainy ◽  
Leslie Solberg ◽  
Mark Poch ◽  
Robin Miller-Catchpole
Keyword(s):  
Ferrous Iron ◽  
Iron Uptake ◽  
Bifidobacterium Bifidum ◽  
Metabolic Inhibitors

scholarly journals Toward a mechanistic understanding of Feo-mediated ferrous iron uptake

Metallomics ◽  
2018 ◽  
Vol 10 (7) ◽  
pp. 887-898 ◽  
Author(s):  
Alexandrea E. Sestok ◽  
Richard O. Linkous ◽  
Aaron T. Smith
Keyword(s):  
Ferrous Iron ◽  
Iron Uptake ◽  
Iron Transport ◽  
Structure And Function ◽  
Ferrous Iron Transport ◽  
Mechanistic Understanding ◽  
And Function

The ferrous iron transport (Feo) system is the predominant mode of bacterial Fe2+import. Advancements in the structure and function of FeoB provide glimpses into the mechanism of Fe2+uptake.

scholarly journals Structure of an atypical FeoB G-domain reveals a putative domain-swapped dimer

2013 ◽  
Vol 69 (4) ◽  
pp. 399-404 ◽  
Author(s):  
Chandrika N. Deshpande ◽  
Aaron P. McGrath ◽  
Josep Font ◽  
Amy P. Guilfoyle ◽  
Megan J. Maher ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Ferrous Iron ◽  
Iron Uptake ◽  
Transmembrane Domain ◽  
Transmembrane Protein ◽  
Gtpase Domain ◽  
Helical Domain ◽  
Precise Role ◽  
Putative Domain

FeoB is a transmembrane protein involved in ferrous iron uptake in prokaryotic organisms. FeoB comprises a cytoplasmic soluble domain termed NFeoB and a C-terminal polytopic transmembrane domain. Recent structures of NFeoB have revealed two structural subdomains: a canonical GTPase domain and a five-helix helical domain. The GTPase domain hydrolyses GTP to GDP through a well characterized mechanism, a process which is required for Fe2+transport. In contrast, the precise role of the helical domain has not yet been fully determined. Here, the structure of the cytoplasmic domain of FeoB fromGallionella capsiferriformansis reported. Unlike recent structures of NFeoB, theG. capsiferriformansNFeoB structure is highly unusual in that it does not contain a helical domain. The crystal structures of both apo and GDP-bound protein forms a domain-swapped dimer.

Premicellar taurocholate enhances ferrous iron uptake from all regions of rat small intestine

1991 ◽  
Vol 101 (2) ◽  
pp. 382-389 ◽  
Author(s):  
Arun J. Sanyal ◽  
Mitchell L. Shiffman ◽  
Jerry I. Hirsch ◽  
Edward W. Moore
Keyword(s):  
Small Intestine ◽  
Ferrous Iron ◽  
Iron Uptake ◽  
Rat Small Intestine

scholarly journals Vibrio cholerae FeoB hydrolyzes ATP and GTP in vitro in the absence of stimulatory factors

Metallomics ◽  
2020 ◽  
Author(s):  
Camilo Gómez-Garzón ◽  
Shelley M. Payne
Keyword(s):  
Vibrio Cholerae ◽  
Ferrous Iron ◽  
Iron Uptake ◽  
Molar Ratio

V. cholerae FeoA, FeoB, and FeoC work at a 1 : 1 : 1 molar ratio to mediate ferrous iron uptake through a mechanism driven by FeoB NTP hydrolysis without requiring stimulatory factors.

A cell biological view of the siderophore pyochelin iron uptake pathway inPseudomonas aeruginosa

2014 ◽  
Vol 17 (1) ◽  
pp. 171-185 ◽  
Author(s):  
Olivier Cunrath ◽  
Véronique Gasser ◽  
Françoise Hoegy ◽  
Cornelia Reimmann ◽  
Laurent Guillon ◽  
...  
Keyword(s):  
Iron Uptake ◽  
Uptake Pathway ◽  
A Cell

scholarly journals Secreted Pyomelanin of Legionella pneumophila Promotes Bacterial Iron Uptake and Growth under Iron-Limiting Conditions

2013 ◽  
Vol 81 (11) ◽  
pp. 4182-4191 ◽  
Author(s):  
Huaixin Zheng ◽  
Christa H. Chatfield ◽  
Mark R. Liles ◽  
Nicholas P. Cianciotto
Keyword(s):  
Legionella Pneumophila ◽  
Ferrous Iron ◽  
Iron Uptake ◽  
Iron Transport ◽  
Ferric Iron ◽  
Iron Acquisition ◽  
Ferric Hydroxide ◽  
Supernatant Fraction ◽  
Content Type ◽  
Ferrous Iron Transport

ABSTRACTIron acquisition is critical to the growth and virulence ofLegionella pneumophila. Previously, we found thatL. pneumophilauses both a ferrisiderophore pathway and ferrous iron transport to obtain iron. We now report that two molecules secreted byL. pneumophila, homogentisic acid (HGA) and its polymerized variant (HGA-melanin, a pyomelanin), are able to directly mediate the reduction of various ferric iron salts. Furthermore, HGA, synthetic HGA-melanin, and HGA-melanin derived from bacterial supernatants enhanced the ability ofL. pneumophilaand other species ofLegionellato take up radiolabeled iron. Enhanced iron uptake was not observed with a ferrous iron transport mutant. Thus, HGA and HGA-melanin mediate ferric iron reduction, with the resulting ferrous iron being available to the bacterium for uptake. Upon further testing ofL. pneumophilaculture supernatants, we found that significant amounts of ferric and ferrous iron were associated with secreted HGA-melanin. Importantly, a pyomelanin-containing fraction obtained from a wild-type culture supernatant was able to stimulate the growth of iron-starved legionellae. That the corresponding supernatant fraction obtained from a nonpigmented mutant culture did not stimulate growth demonstrated that HGA-melanin is able to both promote iron uptake and enhance growth under iron-limiting conditions. Indicative of a complementary role in iron acquisition, HGA-melanin levels were inversely related to the levels of siderophore activity. Compatible with a role in the ecology and pathogenesis ofL. pneumophila, HGA and HGA-melanin were effective at reducing and releasing iron from both insoluble ferric hydroxide and the mammalian iron chelates ferritin and transferrin.

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