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Advances in Metal Metabolism Research 2.0
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Advances in Metal Metabolism Research 2.0

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (20 May 2024) | Viewed by 3668

Special Issue Editor

Prof. Dr. Reinhard Dallinger

E-Mail Website
Guest Editor
Institute of Zoology, University of Innsbruck, Technikerstr. 25, 6020 Innsbruck, Austria
Interests: environmental toxicology and ecotoxicology; molecular physiology; microevolution of metal sensitivity; evolution; biochemistry and gene regulation of metallothioneins; metal-specific pathways in animal physiology; metal detoxification; metal-related biological indicators and biomarkers
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

After the publication of two issues in the International Journal of Molecular Sciences dedicated to “Metal Metabolism in Animals” (in 2016 and 2017), one may ask about the reasonableness of adding a third issue to this series. In fact, the subject of metal metabolism in animals in this journal has so far been treated in a very thorough manner. In the first issue (“Metal Metabolism in Animals I”, edited 2016), articles were dedicated to subjects like the significance of metals, metal-binding features and the role of metals in metalloproteins, metal homeostasis and detoxification, as well as trace element supplementation in animals. In the second issue (“Metal Metabolism in Animals II”, edited 2017), the perspective was extended to human beings with articles focusing on aspects of metal allergy and immunology, models of metal uptake and effects during pregnancy, as well as toxicological and pathological effects of metals on animals and humans.

During the last years, an increasing number of publications has appeared dealing with the molecular evolutionary aspects of metal handling in organisms. Thus, it was shown that in addition to traditional aspects of metallomics, evolutionary approaches could help one to better understand how strategies of metal handling have gradually been shaped through generations and lineages of organisms from all domains of life, and how this may have fostered adaptation to their different environments. This has undoubtedly increased our perception of these processes of adaptation. An evolutionary view may also increase our understanding of how ancestral metal handling features may have been optimized towards more complex and, perhaps, more efficient mechanisms and interconnections.

Although articles dealing with molecular evolutionary aspects of metal metabolism were not explicitly excluded in the former issues, we would like on this occasion to put a particular focus on these subjects, including now living organisms across all domains of life.

Thus, in particular, we welcome articles with a strong molecular and metallomic focus, dealing with the following topics:

  • The molecular evolutionary aspects of mechanisms and strategies of trace-element uptake, regulation, and homeostasis in all kinds or organisms;
  • The evolution of metal-binding proteins and metallo-enzymes, and their interaction with other cellular components through time and across lineages and populations;
  • The evolution of metal regulatory gene-networks;
  • The evolutionary, micro-evolutionary, and population-specific effects of metal handling in all species of organisms, both under laboratory conditions and in the wild;
  • The epigenetic aspects and mechanisms of metal-handling strategies;
  • The effects of metal toxicity under an epigenetic perspective;
  • Evolutionary engineering and optimization in the laboratory or in the field of metal-handling proteins and of genes involved in metal metabolism;
  • Any other topic focusing, in an integrative manner, on the evolution and phylogeny of metal-handling mechanisms and metal metabolism in all kinds of organisms.

Prof. Dr. Reinhard Dallinger
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • molecular evolution
  • phylogeny
  • epigenetics
  • adaptation
  • gene networks
  • metal metabolism
  • metal toxicity
  • metal homeostasis
  • metallo-enzymes and metallo-proteins
  • evolutionary engineering

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Published Papers (2 papers)

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Research

12 pages, 1486 KiB  
Article
The Modular Architecture of Metallothioneins Facilitates Domain Rearrangements and Contributes to Their Evolvability in Metal-Accumulating Mollusks
by Sara Calatayud, Mario Garcia-Risco, Veronika Pedrini-Martha, Michael Niederwanger, Reinhard Dallinger, Òscar Palacios, Mercè Capdevila and Ricard Albalat
Int. J. Mol. Sci. 2022, 23(24), 15824; https://doi.org/10.3390/ijms232415824 - 13 Dec 2022
Cited by 3 | Viewed by 1538
Abstract
Protein domains are independent structural and functional modules that can rearrange to create new proteins. While the evolution of multidomain proteins through the shuffling of different preexisting domains has been well documented, the evolution of domain repeat proteins and the origin of new [...] Read more.
Protein domains are independent structural and functional modules that can rearrange to create new proteins. While the evolution of multidomain proteins through the shuffling of different preexisting domains has been well documented, the evolution of domain repeat proteins and the origin of new domains are less understood. Metallothioneins (MTs) provide a good case study considering that they consist of metal-binding domain repeats, some of them with a likely de novo origin. In mollusks, for instance, most MTs are bidomain proteins that arose by lineage-specific rearrangements between six putative domains: α, β1, β2, β3, γ and δ. Some domains have been characterized in bivalves and gastropods, but nothing is known about the MTs and their domains of other Mollusca classes. To fill this gap, we investigated the metal-binding features of NpoMT1 of Nautilus pompilius (Cephalopoda class) and FcaMT1 of Falcidens caudatus (Caudofoveata class). Interestingly, whereas NpoMT1 consists of α and β1 domains and has a prototypical Cd2+ preference, FcaMT1 has a singular preference for Zn2+ ions and a distinct domain composition, including a new Caudofoveata-specific δ domain. Overall, our results suggest that the modular architecture of MTs has contributed to MT evolution during mollusk diversification, and exemplify how modularity increases MT evolvability. Full article
(This article belongs to the Special Issue Advances in Metal Metabolism Research 2.0)
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16 pages, 4805 KiB  
Article
Evolution of an Iron-Detoxifying Protein: Eukaryotic and Rickettsia Frataxins Contain a Conserved Site Which Is Not Present in Their Bacterial Homologues
by Rui Alves, Maria Pazos-Gil, Marta Medina-Carbonero, Arabela Sanz-Alcázar, Fabien Delaspre and Jordi Tamarit
Int. J. Mol. Sci. 2022, 23(21), 13151; https://doi.org/10.3390/ijms232113151 - 29 Oct 2022
Cited by 1 | Viewed by 1419
Abstract
Friedreich’s ataxia is a neurodegenerative disease caused by mutations in the frataxin gene. Frataxin homologues, including bacterial CyaY proteins, can be found in most species and play a fundamental role in mitochondrial iron homeostasis, either promoting iron assembly into metaloproteins or contributing to [...] Read more.
Friedreich’s ataxia is a neurodegenerative disease caused by mutations in the frataxin gene. Frataxin homologues, including bacterial CyaY proteins, can be found in most species and play a fundamental role in mitochondrial iron homeostasis, either promoting iron assembly into metaloproteins or contributing to iron detoxification. While several lines of evidence suggest that eukaryotic frataxins are more effective than bacterial ones in iron detoxification, the residues involved in this gain of function are unknown. In this work, we analyze conservation of amino acid sequence and protein structure among frataxins and CyaY proteins to identify four highly conserved residue clusters and group them into potential functional clusters. Clusters 1, 2, and 4 are present in eukaryotic frataxins and bacterial CyaY proteins. Cluster 3, containing two serines, a tyrosine, and a glutamate, is only present in eukaryotic frataxins and on CyaY proteins from the Rickettsia genus. Residues from cluster 3 are blocking a small cavity of about 40 Å present in E. coli’s CyaY. The function of this cluster is unknown, but we hypothesize that its tyrosine may contribute to prevent formation of reactive oxygen species during iron detoxification. This cluster provides an example of gain of function during evolution in a protein involved in iron homeostasis, as our results suggests that Cluster 3 was present in the endosymbiont ancestor of mitochondria and was conserved in eukaryotic frataxins. Full article
(This article belongs to the Special Issue Advances in Metal Metabolism Research 2.0)
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