Structure and function of the vacuolar Ccc1/VIT1 family of iron transporters and its regulation in fungi.
BLOSUM, BLOcks SUbstitution Matrix
CBC, CCAAT-binding core complex
CRD, Cysteine-rich domain
CS, Consistency score
Ccc1
Cg, Candida glabrata
Eg, Eucalyptus grandis
Fe, Iron
Fungi
H, Helix
Hap, Heme activator protein
ISC, Iron-sulfur luster
Iron detoxification
Iron regulation
Iron transport
MAFFT, Multiple Alignment using Fast Fourier Transform
MBD, Metal-binding domain
ML, Maximum-likelihood
NRAMP, Natural Resistance-Associated Macrophage Protein
Plants
ROS, Reactive oxygen species
TMD, Transmembrane domain
VIT, Vacuolar iron transporter
VIT1
VTL, Vacuolar iron transporter-like
Vacuole
YRE, Yap response elements
Yeast
bZIP, basic leucine-zipper
Journal
Computational and structural biotechnology journal
ISSN: 2001-0370
Titre abrégé: Comput Struct Biotechnol J
Pays: Netherlands
ID NLM: 101585369
Informations de publication
Date de publication:
2020
2020
Historique:
received:
10
09
2020
revised:
28
10
2020
accepted:
31
10
2020
entrez:
11
12
2020
pubmed:
12
12
2020
medline:
12
12
2020
Statut:
epublish
Résumé
Iron is an essential micronutrient for most living beings since it participates as a redox active cofactor in many biological processes including cellular respiration, lipid biosynthesis, DNA replication and repair, and ribosome biogenesis and recycling. However, when present in excess, iron can participate in Fenton reactions and generate reactive oxygen species that damage cells at the level of proteins, lipids and nucleic acids. Organisms have developed different molecular strategies to protect themselves against the harmful effects of high concentrations of iron. In the case of fungi and plants, detoxification mainly occurs by importing cytosolic iron into the vacuole through the Ccc1/VIT1 iron transporter. New sequenced genomes and bioinformatic tools are facilitating the functional characterization, evolution and ecological relevance of metabolic pathways and homeostatic networks across the Tree of Life. Sequence analysis shows that Ccc1/VIT1 homologs are widely distributed among organisms with the exception of animals. The recent elucidation of the crystal structure of a Ccc1/VIT1 plant ortholog has enabled the identification of both conserved and species-specific motifs required for its metal transport mechanism. Moreover, recent studies in the yeast
Identifiants
pubmed: 33304466
doi: 10.1016/j.csbj.2020.10.044
pii: S2001-0370(20)30466-9
pmc: PMC7714665
doi:
Types de publication
Journal Article
Review
Langues
eng
Pagination
3712-3722Informations de copyright
© 2020 The Authors. Published by Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology.
Déclaration de conflit d'intérêts
The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
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