Cloning of Pichia pastoris Fet3: Insights into the High Affinity Iron Uptake System

2001 ◽  
Vol 392 (1) ◽  
pp. 162-167 ◽  
Author(s):  
Maria Paola Paronetto ◽  
Rossella Miele ◽  
Antonella Maugliani ◽  
Marina Borro ◽  
Maria Carmela Bonaccorsi di Patti
Keyword(s):  
Pichia Pastoris ◽  
Iron Uptake ◽  
Uptake System ◽  
High Affinity ◽  
Iron Uptake System

scholarly journals Yeast protective response to arsenate involves the repression of the high affinity iron uptake system

2013 ◽  
Vol 1833 (5) ◽  
pp. 997-1005 ◽  
Author(s):  
Liliana Batista-Nascimento ◽  
Michel B. Toledano ◽  
Dennis J. Thiele ◽  
Claudina Rodrigues-Pousada
Keyword(s):  
Iron Uptake ◽  
Uptake System ◽  
Protective Response ◽  
High Affinity ◽  
Iron Uptake System

scholarly journals Dual Regulation of the Arabidopsis High-Affinity Root Iron Uptake System by Local and Long-Distance Signals

2003 ◽  
Vol 132 (2) ◽  
pp. 796-804 ◽  
Author(s):  
Grégory A. Vert ◽  
Jean-François Briat ◽  
Catherine Curie
Keyword(s):  
Iron Uptake ◽  
Uptake System ◽  
Long Distance ◽  
High Affinity ◽  
Iron Uptake System

scholarly journals Biosynthesis and Uptake of Siderophores Is Controlled by the PacC-Mediated Ambient-pH Regulatory System in Aspergillus nidulans

2004 ◽  
Vol 3 (2) ◽  
pp. 561-563 ◽  
Author(s):  
Martin Eisendle ◽  
Harald Oberegger ◽  
Rudolf Buttinger ◽  
Paul Illmer ◽  
Hubertus Haas
Keyword(s):  
Aspergillus Nidulans ◽  
Iron Uptake ◽  
Regulatory System ◽  
Transcriptional Regulator ◽  
Uptake System ◽  
Iron Availability ◽  
High Affinity ◽  
Iron Uptake System

ABSTRACT Biosynthesis and uptake of siderophores in Aspergillus nidulans are regulated not only by iron availability but also by ambient pH: expression of this high-affinity iron uptake system is elevated by an increase in the ambient pH. Mediation of this regulation by the transcriptional regulator PacC has been confirmed via acidity- and alkalinity-mimicking mutants.

scholarly journals Iron restriction and the growth ofSalmonella enteritidis

1993 ◽  
Vol 110 (1) ◽  
pp. 41-47 ◽  
Author(s):  
H. Chart ◽  
B. Rowe
Keyword(s):  
Iron Uptake ◽  
Salmonella Enteritidis ◽  
Outer Membrane Proteins ◽  
Phage Type ◽  
Iron Chelator ◽  
Virulence Plasmid ◽  
Uptake System ◽  
Iron Restriction ◽  
High Affinity ◽  
Iron Uptake System

SUMMARYStrains ofSalmonella enteritidiswere examined for their ability to remove ferricions from the iron chelating agents ovotransferrin, Desferal and EDDA. Growth ofS. enteritidisphage type (PT) 4 (SE4) in trypticase soy broth containing ovotransferrin resulted in the expression of iron regulated outer membrane proteins (OMPs) of 74. 78 and 81 kDa. and unexpectedly the repression of expression of OMP C. The 38 MDa ‘mouse virulence’ plasmid was not required for the expression of the iron-regulated OMPs (IROMPs). SE4 was able to obtain iron bound to the iron chelator Desferal and EDDA without expressing a high-affinity iron uptake system. Strains ofS. enteritidisbelonging to PTs 7. 8, 13a, 23. 24 and 30 were also able to remove ferric ions from Desferal and EDDA without expressing a high-affinity iron uptake system. We conclude that strains of SE4 possess a high-affinity iron sequestering mechanism that can readily remove iron from ovotransferrin. It is likely that iron limitation, and not iron restriction, is responsible for the bacteriostatic properties of fresh egg whites.

scholarly journals Evidence thatYersinia ruckeripossesses a high affinity iron uptake system

1991 ◽  
Vol 80 (2-3) ◽  
pp. 121-126 ◽  
Author(s):  
Jesús L. Romalde ◽  
Ramón F. Conchas ◽  
Alicia E. Toranzo
Keyword(s):  
Iron Uptake ◽  
Uptake System ◽  
High Affinity ◽  
Iron Uptake System

scholarly journals Two Iron-Responsive Promoter Elements Control Expression of FOX1 in Chlamydomonas reinhardtii

2007 ◽  
Vol 6 (11) ◽  
pp. 2163-2167 ◽  
Author(s):  
Xiaodong Deng ◽  
Mats Eriksson
Keyword(s):  
Iron Deficiency ◽  
Chlamydomonas Reinhardtii ◽  
Iron Uptake ◽  
Uptake System ◽  
Promoter Elements ◽  
High Affinity ◽  
Iron Uptake System ◽  
Iron Responsive Elements

ABSTRACT FOX1 encodes an iron deficiency-induced ferroxidase involved in a high-affinity iron uptake system. Mutagenesis analysis of the FOX1 promoter identified two separate iron-responsive elements, FeRE1 (CACACG) and FeRE2 (CACGCG), between positions −87 and −82 and between positions −65 and −60, respectively, and both are needed for induced FOX1 expression under conditions of iron deficiency.

Arabidopsis IRT2 cooperates with the high-affinity iron uptake system to maintain iron homeostasis in root epidermal cells

Planta ◽  
2009 ◽  
Vol 229 (6) ◽  
pp. 1171-1179 ◽  
Author(s):  
Grégory Vert ◽  
Marie Barberon ◽  
Enric Zelazny ◽  
Mathilde Séguéla ◽  
Jean-François Briat ◽  
...  
Keyword(s):  
Iron Uptake ◽  
Iron Homeostasis ◽  
Epidermal Cells ◽  
Uptake System ◽  
High Affinity ◽  
Iron Uptake System

Evidence for a copper-dependent iron transport system in the marine, magnetotactic bacterium strain MV-1

Microbiology ◽  
2004 ◽  
Vol 150 (9) ◽  
pp. 2931-2945 ◽  
Author(s):  
Bradley L. Dubbels ◽  
Alan A. DiSpirito ◽  
John D. Morton ◽  
Jeremy D. Semrau ◽  
J. N. E. Neto ◽  
...  
Keyword(s):  
Iron Content ◽  
Iron Uptake ◽  
Iron Transport ◽  
Dna Analysis ◽  
Iron Concentration ◽  
Protein A ◽  
Uptake System ◽  
Iron Uptake System ◽  
Cellular Iron ◽  
Solid Media

Cells of the magnetotactic marine vibrio, strain MV-1, produce magnetite-containing magnetosomes when grown anaerobically or microaerobically. Stable, spontaneous, non-magnetotactic mutants were regularly observed when cells of MV-1 were cultured on solid media incubated under anaerobic or microaerobic conditions. Randomly amplified polymorphic DNA analysis showed that these mutants are not all genetically identical. Cellular iron content of one non-magnetotactic mutant strain, designated MV-1nm1, grown anaerobically, was ∼20- to 80-fold less than the iron content of wild-type (wt) MV-1 for the same iron concentrations, indicating that MV-1nm1 is deficient in some form of iron uptake. Comparative protein profiles of the two strains showed that MV-1nm1 did not produce several proteins produced by wt MV-1. To understand the potential roles of these proteins in iron transport better, one of these proteins was purified and characterized. This protein, a homodimer with an apparent subunit mass of about 19 kDa, was an iron-regulated, periplasmic protein (p19). Two potential ‘copper-handling’ motifs (MXM/MX2M) are present in the amino acid sequence of p19, and the native protein binds copper in a 1 : 1 ratio. The structural gene for p19, chpA (copper handling protein) and two other putative genes upstream of chpA were cloned and sequenced. These putative genes encode a protein similar to the iron permease, Ftr1, from the yeast Saccharomyces cerevisiae, and a ferredoxin-like protein of unknown function. A periplasmic, copper-containing, iron(II) oxidase was also purified from wt MV-1 and MV-1nm1. This enzyme, like p19, was regulated by media iron concentration and contained four copper atoms per molecule of enzyme. It is hypothesized that ChpA, the iron permease and the iron(II) oxidase might have analogous functions for the three components of the S. cerevisiae copper-dependent high-affinity iron uptake system (Ctr1, Ftr1 and Fet3, respectively), and that strain MV-1 may have a similar iron uptake system. However, iron(II) oxidase purified from both wt MV-1 and MV-1nm1 displayed comparable iron oxidase activities using O2 as the electron acceptor, indicating that ChpA does not supply the multi-copper iron(II) oxidase with copper.

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