Signaling Pathways of Metallic Micronutrient Homeostasis in Photosynthetic Organisms

A special issue of Plants (ISSN 2223-7747). This special issue belongs to the section "Plant Nutrition".

Deadline for manuscript submissions: closed (30 April 2022) | Viewed by 3479

Special Issue Editors


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Centre for Photosynthetic and Biochemical Studies, National University of Rosario, Rosario 2000, Argentina
Interests: plant biotechnology; plant mitochondria; starch; enzyme structure and regulation
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Guest Editor
Faculty of Biological Sciences, Pontificia Universidad Católica de Chile, Santiago de Chile, Chile
Interests: iron metabolism; seed metal metabolism

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Centro de Estudios Fotosintéticos y Bioquímicos (CEFOBI-CONICET), Universidad Nacional de Rosario, Rosario S2000CGK, Santa Fe, Argentina
Interests: metallothioneins; iron signalling; iron metabolism in plants; micronutrients

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CEFOBI–CONICET–UNR, Suipacha 570, Rosario 2000, Argentina
Interests: starch metabolism; polysaccharides metabolism; algae; plants; enzymes; carbohydrate-binding modules; starch-binding modules; biotechnological applications
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Most metals are essential micronutrients in all organisms. Metal metabolism is not only important at the agronomic level in plants, but also for human health. In photosynthetic organisms, metals such as iron and copper fulfill various functions related to mitochondrial respiration, photosynthesis, DNA synthesis, maintenance of the structure and function of organelles, and redox metabolism. Although many metals can sometimes be abundant in many soils, the low availability of some of them, such as Fe, has a negative effect on plant growth and development. In contrast, excess of metals is toxic to plants, and therefore, the levels of these micronutrients in cells must be strictly regulated. This Special Volume will highlight the different aspects of metal uptake, utilization, regulation, and signaling in photosynthetic organisms.

Prof. Dr. Diego F. Gomez-Casati
Dr. Hannetz Roschzttardtz
Dr. Maria Ayelén Pagani
Dr. Maria Victoria Busi
Guest Editors

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Keywords

  • metal homeostasis
  • micronutrients
  • metal signaling
  • photosynthetic organisms

Published Papers (2 papers)

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Research

16 pages, 4868 KiB  
Article
Structural and Functional Characterization of CreFH1, the Frataxin Homolog from Chlamydomonas reinhardtii
by Agustina Terenzi, Maria A. Pagani, Diego F. Gomez-Casati and Maria V. Busi
Plants 2022, 11(15), 1931; https://doi.org/10.3390/plants11151931 - 26 Jul 2022
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Abstract
Frataxin plays a key role in cellular iron homeostasis of different organisms. It has been implicated in iron storage, detoxification, delivery for Fe-S cluster assembly and heme biosynthesis. However, its specific role in iron metabolism remains unclear, especially in photosynthetic organisms. To gain [...] Read more.
Frataxin plays a key role in cellular iron homeostasis of different organisms. It has been implicated in iron storage, detoxification, delivery for Fe-S cluster assembly and heme biosynthesis. However, its specific role in iron metabolism remains unclear, especially in photosynthetic organisms. To gain insight into the role and properties of frataxin in algae, we identified the gene CreFH1, which codes for the frataxin homolog from Chlamydomonas reinhardtii. We performed the cloning, expression and biochemical characterization of CreFH1. This protein has a predicted mitochondrial transit peptide and a significant structural similarity to other members of the frataxin family. In addition, CreFH1 was able to form a dimer in vitro, and this effect was increased by the addition of Cu2+ and also attenuated the Fenton reaction in the presence of a mixture of Fe2+ and H2O2. Bacterial cells with overexpression of CreFH1 showed increased growth in the presence of different metals, such as Fe, Cu, Zn and Ni and H2O2. Thus, results indicated that CreFH1 is a functional protein that shows some distinctive features compared to its more well-known counterparts, and would play an important role in response to oxidative stress in C. reinhardtii. Full article
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10 pages, 1576 KiB  
Article
Effects of Magnesium, Pyrophosphate and Phosphonates on Pyrophosphorolytic Reaction of UDP-Glucose Pyrophosphorylase
by Leszek A. Kleczkowski and Daniel Decker
Plants 2022, 11(12), 1611; https://doi.org/10.3390/plants11121611 - 20 Jun 2022
Cited by 3 | Viewed by 1600
Abstract
UDP-glucose pyrophosphorylase (UGPase) carries a freely reversible reaction, using glucose-1-P and UTP to produce UDP-glucose (UDPG) and pyrophosphate (PPi), with UDPG being essential for glycosylation reactions in all organisms including, e.g., synthesis of sucrose, cellulose and glycoproteins. In the present study, [...] Read more.
UDP-glucose pyrophosphorylase (UGPase) carries a freely reversible reaction, using glucose-1-P and UTP to produce UDP-glucose (UDPG) and pyrophosphate (PPi), with UDPG being essential for glycosylation reactions in all organisms including, e.g., synthesis of sucrose, cellulose and glycoproteins. In the present study, we found that free magnesium (Mg2+) had profound effects on the reverse reaction of purified barley UGPase, and was absolutely required for its activity, with an apparent Km of 0.13 mM. More detailed analyses with varied concentrations of MgPPi allowed us to conclude that it is the MgPPi complex which serves as true substrate for UGPase in its reverse reaction, with an apparent Km of 0.06 mM. Free PPi was an inhibitor in this reaction. Given the key role of PPi in the UGPase reaction, we have also tested possible effects of phosphonates, which are analogs of PPi and phosphate (Pi). Clodronate and etidronate (PPi analogs) had little or no effect on UGPase activity, whereas fosetyl-Al (Pi analog), a known fungicide, acted as effective near-competitive inhibitor versus PPi, with Ki of 0.15 mM. The data are discussed with respect to the role of magnesium in the UGPase reaction and elucidating the use of inhibitors in studies on cellular function of UGPase and related enzymes. Full article
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