Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.16.3.1 (ceruloplasmin)
5,074 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
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PMID:Two iron-responsive promoter elements control expression of FOX1 in Chlamydomonas reinhardtii. 1790 21

Chlamydomonas, like other organisms, regulates iron assimilation very tightly through differential expression of iron assimilation components. Nevertheless, in the presence of excess iron, cells do overaccumulate iron but without an evident phenotype. As iron toxicity is attributed to reactive oxygen species, we tested the impact of photon flux density (PFD) on cells with increased iron content. We noted that growth at > 500 micromol m(-2) s(-1) is inhibited as iron content of the medium is increased, suggesting that high light exacerbates the systems of iron toxicity and vice versa. Cells grown in high light selectively down-regulate the abundance of iron assimilation components, ferroxidase and FEA1, and storage protein ferritin1. At the RNA level, the abundance of ferroxidase (FOX1), iron reductase (FRE1), iron assimilatory protein (FEA1) and ferritin (FER1) mRNAs is also decreased. The time course of the response to high light compared to the response to Rose Bengal and H2O2 treatments suggests that both singlet oxygen and H2O2 may be implicated in the high light response. This hypothesis is supported by the recapitulation of some but not all of the high light responses in the carotenoid-deficient, high light-sensitive npq1lor1 strain. We conclude that responses to iron nutrition and PFD are connected, and the determination of an optimum for photosynthetic growth for each is dependent on the other. This work defines a fourth stage of iron nutrition in Chlamydomonas, the iron excess situation, which can be molecularly and physiologically distinguished from the iron-limited, iron-deficient and iron-replete stages, described previously.
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PMID:Photo-oxidative stress impacts the expression of genes encoding iron metabolism components in Chlamydomonas. 1906 61

Multicopper ferroxidases play a vital role in iron metabolism in bacteria, fungi, algae, and mammals. Saccharomyces cerevisiae utilizes a channeling mechanism to couple the ferroxidase activity of Fet3p to Fe(3+) transport into the cell by Ftr1p. In contrast, the mechanisms by which mammals couple the ferroxidase reaction to iron trafficking is unclear. The human ferroxidases ceruloplasmin and hephaestin are twice the size of Fet3p and interact with proteins that are not expressed in fungi. Chlamydomonas FOX1 is a homolog of the human ferroxidases but likely supports iron uptake in a manner similar to that of yeast, since Chlamydomonas reinhardtii expresses a ferric iron permease homolog, FTR1. The results presented support this hypothesis. We show that FOX1 is trafficked to the plasma membrane and is oriented with its multicopper oxidase/ferroxidase domain in the exocytoplasmic space. Our analysis of FTR1 indicates its topology is similar to that of S. cerevisiae Ftr1p, with a potential exocytoplasmic iron channeling motif and two potential iron permeation motifs in membrane-spanning regions. We demonstrate that high-affinity iron uptake is dependent on FOX1 and the copper status of the cell. Kinetic inhibition of high-affinity iron uptake by a ferric iron chelator does not reflect the strength of the chelator, supporting a ferric iron channeling mechanism for high-affinity iron uptake in Chlamydomonas. Last, recombinant FOX1 (rFOX1) has been isolated in a partially holo form that exhibits the UV-visible absorbance spectrum of a multicopper oxidase and the catalytic activity of a ferroxidase.
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PMID:Analysis of the high-affinity iron uptake system at the Chlamydomonas reinhardtii plasma membrane. 2034 89