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Review
. 2021 Sep 30:9:735678.
doi: 10.3389/fcell.2021.735678. eCollection 2021.

Biogenesis of Iron-Sulfur Clusters and Their Role in DNA Metabolism

Ruifeng Shi  1   2 , Wenya Hou  2 , Zhao-Qi Wang  3   4 , Xingzhi Xu  1   2
Affiliations
Review

Biogenesis of Iron-Sulfur Clusters and Their Role in DNA Metabolism

Ruifeng Shi et al. Front Cell Dev Biol. .

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.

Keywords: DNA metabolism; DNA repair; DNA replication; genome stability; iron-sulfur (Fe-S) clusters.

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Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

FIGURE 1
FIGURE 1
Different possible structures of Fe/S clusters. (A) The structure of the rhombic 2Fe–2S cluster; (B) the structure of the cubane 4Fe–4S cluster.
See this image and copyright information in PMC

References

    1. Adamec J., Rusnak F., Owen W. G., Naylor S., Benson L. M., Gacy A. M., et al. (2000). Iron-dependent self-assembly of recombinant yeast frataxin: implications for Friedreich ataxia. Am. J. Hum. Genet. 67 549–562. 10.1086/303056 - DOI - PMC - PubMed
    1. Alseth I., Eide L., Pirovano M., Rognes T., Seeberg E., Bjoras M. (1999). The Saccharomyces cerevisiae homologues of endonuclease III from Escherichia coli, Ntg1 and Ntg2, are both required for efficient repair of spontaneous and induced oxidative DNA damage in yeast. Mol. Cell Biol. 19 3779–3787. 10.1128/mcb.19.5.3779 - DOI - PMC - PubMed
    1. Andreini C., Rosato A., Banci L. (2017). The relationship between environmental dioxygen and iron-sulfur proteins explored at the genome level. PLoS One 12:e0171279. 10.1371/journal.pone.0171279 - DOI - PMC - PubMed
    1. Arnold A. R., Grodick M. A., Barton J. K. (2016). DNA charge transport: from chemical principles to the cell. Cell Chem. Biol. 23 183–197. 10.1016/j.chembiol.2015.11.010 - DOI - PMC - PubMed
    1. Askree S. H., Yehuda T., Smolikov S., Gurevich R., Hawk J., Coker C., et al. (2004). A genome-wide screen for Saccharomyces cerevisiae deletion mutants that affect telomere length. Proc. Natl. Acad. Sci. U.S.A. 101 8658–8663. 10.1073/pnas.0401263101 - DOI - PMC - PubMed