Iron deprivation decreases ribonucleotide reductase activity and DNA synthesis
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NCOA4 links iron bioavailability to DNA metabolism
2022, Cell ReportsToxicity of the iron siderophore mycobactin J in mouse macrophages: Evidence for a hypoxia response
2022, Journal of Inorganic BiochemistryCitation Excerpt :Further searching reveals that 25 of the 38 genes have been linked to hypoxia (Table 2). This hypoxia-like response is a known effect of iron chelation, due to removal of catalytic iron from prolyl-4-hydroxylases (P4ha1, P4ha2, Egln1 and Egln3 in Fig. 3 and Table 2) [40a,41]. Under normal conditions, prolyl-hydroxylases utilize their catalytic iron centers to hydroxylate HIF-1α, which leads to HIF-1α degradation.
When less is more: Novel mechanisms of iron conservation
2013, Trends in Endocrinology and MetabolismCitation Excerpt :A number of studies in humans and animals have revealed a link between reduced systemic iron and a vast array of gross physiologic abnormalities, including delayed development, reduced physical endurance and mental cognition, immune dysfunction, and impaired thermoregulation [5–7]. In addition to its well-recognized role in oxygen and carbon dioxide transport as a part of the hemoglobin molecule, iron serves as an essential cofactor for a number of critical enzymes that regulate virtually all aspects of cellular and whole-body physiology, including mitochondrial respiration and energy production [8], DNA replication and repair [9,10], protein and lipid biosynthesis [11,12], antioxidation and detoxification of foreign compounds [13,14], and more. Insufficient iron stores can potentially disrupt these processes, particularly in iron-rich tissues such as the brain, heart, and hematopoietic system.
Iron and genome stability: An update
2012, Mutation Research - Fundamental and Molecular Mechanisms of MutagenesisCitation Excerpt :Regarding nucleic acid metabolism, iron is a co-factor of ribonucleotide reductase [31], a DNA primase [32], a DNA glycosylase [26], a DNA endonuclease, an alkyltransferase [21] and DNA helicases [25]. Iron deprivation was shown to reduce ribonucleotide reductase activity, DNA synthesis and cell proliferation [31]. In certain DNA repair enzymes (XPD, FANCJ, MUTYH, NTHL1) Fe–S cluster seems to be involved in the recognition of DNA damage or in another functions [25].
Regulation of ribonucleotide reductase in response to iron deficiency
2011, Molecular CellCitation Excerpt :Such a substitution is not possible in eukaryotes because the only RNR enzyme available fully depends on Fe as a cofactor. In mammals, a severe reduction in Fe bioavailability leads to significant decreases in RNR activity, dNTP pools, DNA synthesis, and consequently cell proliferation (Cavanaugh et al., 1985; Furukawa et al., 1992). Interestingly, in some cases RNR activity seems to be maintained or increased during the early stages of Fe deficiency (Furukawa et al., 1992), suggesting that cells may possess strategies to optimize the essential function of RNR over other less important Fe-using pathways when Fe becomes limiting.