Abstract
Iron–sulfur (Fe/S) clusters (ISCs) are redox-active protein cofactors that their synthesis, transfer, and insertion into target proteins require many components. Mitochondrial ISC assembly is the foundation of all cellular ISCs in eukaryotic cells. The mitochondrial ISC cooperates with the cytosolic Fe/S protein assembly (CIA) systems to accomplish the cytosolic and nuclear Fe/S clusters maturation. ISCs are needed for diverse cellular functions, including nitrogen fixation, oxidative phosphorylation, mitochondrial respiratory pathways, and ribosome assembly. Recent research advances have confirmed the existence of different ISCs in enzymes that regulate DNA metabolism, including helicases, nucleases, primases, DNA polymerases, and glycosylases. Here we outline the synthesis of mitochondrial, cytosolic and nuclear ISCs and highlight their functions in DNA metabolism.
Highlights
Iron–sulfur (Fe/S) clusters (ISCs) are extremely ancient, small inorganic protein cofactors found in almost all organisms
Many biochemical studies demonstrate that methyl methanesulfonate-sensitivity protein 19 (MMS19) and other cytosolic Fe/S protein assembly (CIA) complex components directly interact with diverse DNA metabolism enzymes, such as DNA helicases [XPD, FANCJ (Fanconi anemia complementation group J)], and RTEL1, DNA polymerase subunits (POLD1, POLA1, and POLE1), the nuclease DNA2, the DNA glycosylase NTHL1, and the DNA primase PRI2
The 4Fe–4S cluster is crucial for stabilizing the polymerase complex (Baranovskiy et al, 2018). These findings suggest that the proper activities of DNA polymerases require 4Fe–4S cluster coordination
Summary
Iron–sulfur (Fe/S) clusters (ISCs) are extremely ancient, small inorganic protein cofactors found in almost all organisms. To mitochondrial ISC biogenesis system, the cytoplasm contains different machineries to assembly 4Fe–4S clusters. Similar to ISC biogenesis in mitochondria, the initial step of cytosolic and nuclear ISC synthesis is transient transfer a 4Fe–4S cluster to the cytosolic scaffold protein complex.
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