Dissecting plant iron homeostasis under short and long-term iron fluctuations

Darbani, Behrooz; Briat, Jean‐François; Holm, Preben Bach; Husted, Søren; Noeparvar, Shahin; Borg, Søren

doi:10.1016/j.biotechadv.2013.05.003

Cited by 56 publications

(52 citation statements)

References 265 publications

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“…Glutathione-associated NO-mediated S-nitrosylation of proteins, and their roles in the stress response, were recently reported (Astier et al, 2012;Romero-Puertas et al, 2013). Interestingly, several proteins involved in Fe homeostasis, including basic helix-loop-helix group transcription factors bHLH38 and bHLH39, possess S-nitrosylation motifs (Darbani et al, 2013). The transcription factors bHLH38 or bHLH39 act together with FIT to induce the expression of IRT1 and FRO2 under Fe deficiency (Yuan et al, 2008).…”

Section: Glutathione Is Essential For No-mediated Fe-acquisition/ Defmentioning

confidence: 98%

Glutathione plays an essential role in nitric oxide‐mediated iron‐deficiency signaling and iron‐deficiency tolerance in Arabidopsis

et al. 2015

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Summary Iron (Fe) deficiency is a common agricultural problem that affects both the productivity and nutritional quality of plants. Thus, identifying the key factors involved in the tolerance of Fe deficiency is important. In the present study, the zir1 mutant, which is glutathione deficient, was found to be more sensitive to Fe deficiency than the wild type, and grew poorly in alkaline soil. Other glutathione‐deficient mutants also showed various degrees of sensitivity to Fe‐limited conditions. Interestingly, we found that the glutathione level was increased under Fe deficiency in the wild type. By contrast, blocking glutathione biosynthesis led to increased physiological sensitivity to Fe deficiency. On the other hand, overexpressing glutathione enhanced the tolerance to Fe deficiency. Under Fe‐limited conditions, glutathione‐deficient mutants, zir1, pad2 and cad2 accumulated lower levels of Fe than the wild type. The key genes involved in Fe uptake, including IRT1, FRO2 and FIT, are expressed at low levels in zir1; however, a split‐root experiment suggested that the systemic signals that govern the expression of Fe uptake‐related genes are still active in zir1. Furthermore, we found that zir1 had a lower accumulation of nitric oxide (NO) and NO reservoir S‐nitrosoglutathione (GSNO). Although NO is a signaling molecule involved in the induction of Fe uptake‐related genes during Fe deficiency, the NO‐mediated induction of Fe‐uptake genes is dependent on glutathione supply in the zir1 mutant. These results provide direct evidence that glutathione plays an essential role in Fe‐deficiency tolerance and NO‐mediated Fe‐deficiency signaling in Arabidopsis.

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Section: Glutathione Is Essential For No-mediated Fe-acquisition/ Defmentioning

confidence: 98%

Glutathione plays an essential role in nitric oxide‐mediated iron‐deficiency signaling and iron‐deficiency tolerance in Arabidopsis

et al. 2015

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“…Grasses employ a different mode (termed strategy II) than all other plant groups to actively take up Fe from soils (Mori, 1999;Darbani et al, 2013;Colombo et al, 2014). Grasses excrete phytosiderophores such as mugineic acid or avenic acid that complex Fe 3þ .…”

Section: Iron As An Essential Growth Element Of Plantsmentioning

confidence: 99%

The lime–silicate question

Bothe

2015

Soil Biology and Biochemistry

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“…Di-iron catalytic sites in ferritin protein cages consume the Fe and O substrates that are also the genetic signals, shutting down ferritin gene transcription and ferritin mRNA translation/protein synthesis 84 . When plants, animals or people are iron deficient ferritin synthesis is diminished, but in plants ferritin iron-dependent ferritin regulation is restricted to mRNA synthesis 85 . The critical nature of ferritin to animal life is emphasized by the unique metabolite signal/gene/protein substrate feedback loop and by the embryonic lethality of gene deletions in mice 86 .…”

Section: Regulated Ferritin Protein Biosynthesis (Role Of Mrna Strmentioning

confidence: 99%

Ferritin: The Protein Nanocage and Iron Biomineral in Health and in Disease

2013

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At the center of iron and oxidant metabolism is the ferritin superfamily: protein cages with Fe2+ ion channels and catalytic di- Fe/O redox centers that initiate formation of caged Fe2O3 • H2O. Ferritin nanominerals, initiated within the protein cage, grow inside the cage cavity (5 or 8 nm in diameter). Ferritins contribute to normal iron flow, maintenance of iron concentrates for iron cofactor syntheses, sequestration of iron from invading pathogens, oxidant protection, oxidative stress recovery and, in diseases where iron accumulates excessively, to iron chelation strategies. In eukaryotic ferritins, biomineral order/crystallinity is influenced by nucleation channels between active sites and the mineral growth cavity. Animal ferritin cages contain, uniquely, mixtures of catalytically active (H) and inactive (L) polypeptide subunits with varied rates of Fe2+/O2 catalysis and mineral crystallinity. The relatively low mineral order in liver ferritin, for example, coincides with a high % of L subunits, and, thus, a low % of catalytic sites and nucleation channels. Low mineral order facilitates rapid iron turnover and the physiological role of liver ferritin as a general iron source for other tissues. Here, current concepts of ferritin structure/function/genetic regulation are discussed and related to possible therapeutic targets such as mini-ferritin/Dps protein active sites (selective pathogen inhibition in infection), the nanocage pores (iron chelation in therapeutic hypertransfusion), the mRNA noncoding, IRE-riboregulator (normalizing ferritin iron content after therapeutic hypertransfusion, and as protein nanovessels to deliver medicinal or sensor cargo.

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Dissecting plant iron homeostasis under short and long-term iron fluctuations

Cited by 56 publications

References 265 publications

Glutathione plays an essential role in nitric oxide‐mediated iron‐deficiency signaling and iron‐deficiency tolerance in Arabidopsis

Glutathione plays an essential role in nitric oxide‐mediated iron‐deficiency signaling and iron‐deficiency tolerance in Arabidopsis

The lime–silicate question

Ferritin: The Protein Nanocage and Iron Biomineral in Health and in Disease

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