Eukaryotic DNA polymerases require an iron-sulfur cluster for the formation of active complexes

Netz, Daili J. A.; Stith, Carrie M.; Stümpfig, Martin; Köpf, Gabriele; Vogel, Daniel; Genau, Heide Marika; Stodola, Joseph L.; Lill, Roland; Burgers, Peter M.; Pierik, Antonio J.

doi:10.1038/nchembio.721

Cited by 336 publications

(450 citation statements)

References 49 publications

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“…Such stoichiometry is close to what is typically observed for proteins containing [4Fe-4S] clusters, taking into account that one or two iron atoms per molecule were lost during purification (28,29). Our data are consistent with the recent finding of [4Fe-4S] clusters in yeast Pol ␦ and Pol (30), in human and yeast primases (29,31), and in several proteins involved in DNA repair (26 -28, 32).…”

Section: Structural Similarities Of Ctds Of Catalytic Subunits Of Pol ␦supporting

confidence: 81%

DNA Polymerase δ and ζ Switch by Sharing Accessory Subunits of DNA Polymerase δ

Baranovskiy

Lada

Siebler

et al. 2012

Journal of Biological Chemistry

146

228

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Background: DNA polymerase (Pol) ␦ is involved in UV light-induced mutagenesis by an unknown mechanism. Results: The C terminus of DNA Pol interacts with accessory subunits of DNA Pol ␦, which is required for UV light-induced mutagenesis. Conclusion: When replication is stalled, accessory subunits of DNA Pol ␦ participate in recruitment of translesion DNA Pol . Significance: This finding provides a novel mechanism of DNA lesion bypass in eukaryotes.

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Section: Structural Similarities Of Ctds Of Catalytic Subunits Of Pol ␦supporting

confidence: 81%

DNA Polymerase δ and ζ Switch by Sharing Accessory Subunits of DNA Polymerase δ

Baranovskiy

Lada

Siebler

et al. 2012

Journal of Biological Chemistry

146

228

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“…These observations are now understood because replicative DNA polymerases have been shown to require an Fe-S cluster [50]. However, differences between eukaryote species have also been observed.…”

Section: Discussionmentioning

confidence: 94%

Requirements of the cytosolic iron–sulfur cluster assembly pathway in Arabidopsis

Bernard

Netz

Lagny

et al. 2013

Phil. Trans. R. Soc. B

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The assembly of iron–sulfur (Fe–S) clusters requires dedicated protein factors inside the living cell. Striking similarities between prokaryotic and eukaryotic assembly proteins suggest that plant cells inherited two different pathways through endosymbiosis: the ISC pathway in mitochondria and the SUF pathway in plastids. Fe–S proteins are also found in the cytosol and nucleus, but little is known about how they are assembled in plant cells. Here, we show that neither plastid assembly proteins nor the cytosolic cysteine desulfurase ABA3 are required for the activity of cytosolic aconitase, which depends on a [4Fe–4S] cluster. In contrast, cytosolic aconitase activity depended on the mitochondrial cysteine desulfurase NFS1 and the mitochondrial transporter ATM3. In addition, we were able to complement a yeast mutant in the cytosolic Fe–S cluster assembly pathway, dre2 , with the Arabidopsis homologue AtDRE2 , but only when expressed together with the diflavin reductase AtTAH18 . Spectroscopic characterization showed that purified AtDRE2 could bind up to two Fe–S clusters. Purified AtTAH18 bound one flavin per molecule and was able to accept electrons from NAD(P)H. These results suggest that the proteins involved in cytosolic Fe–S cluster assembly are highly conserved, and that dependence on the mitochondria arose before the second endosymbiosis event leading to plastids.

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“…Besides primases and FeS-BCPs, several other DNA-interacting proteins contain Fe-S clusters (30)(31)(32). Fe-S clusters are regarded as ancient features.…”

Section: Resultsmentioning

confidence: 99%

Crystal structure of a prokaryotic (6-4) photolyase with an Fe-S cluster and a 6,7-dimethyl-8-ribityllumazine antenna chromophore

Zhang

Scheerer

Oberpichler

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

178

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The (6-4) photolyases use blue light to reverse UV-induced (6-4) photoproducts in DNA. This (6-4) photorepair was thought to be restricted to eukaryotes. Here we report a prokaryotic (6-4) photolyase, PhrB from Agrobacterium tumefaciens, and propose that (6-4) photolyases are broadly distributed in prokaryotes. The crystal structure of photolyase related protein B (PhrB) at 1.45 Å resolution suggests a DNA binding mode different from that of the eukaryotic counterparts. A His-His-X-X-Arg motif is located within the proposed DNA lesion contact site of PhrB. This motif is structurally conserved in eukaryotic (6-4) photolyases for which the second His is essential for the (6-4) photolyase function. The PhrB structure contains 6,7-dimethyl-8-ribityllumazine as an antenna chromophore and a [4Fe-4S] cluster bound to the catalytic domain. A significant part of the Fe-S fold strikingly resembles that of the large subunit of eukaryotic and archaeal primases, suggesting that the PhrB-like photolyases branched at the base of the evolution of the cryptochrome/photolyase family. Our study presents a unique prokaryotic (6-4) photolyase and proposes that the prokaryotic (6-4) photolyases are the ancestors of the cryptochrome/photolyase family.DNA repair | UV light | energy transfer

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Eukaryotic DNA polymerases require an iron-sulfur cluster for the formation of active complexes

Cited by 336 publications

References 49 publications

DNA Polymerase δ and ζ Switch by Sharing Accessory Subunits of DNA Polymerase δ

DNA Polymerase δ and ζ Switch by Sharing Accessory Subunits of DNA Polymerase δ

Requirements of the cytosolic iron–sulfur cluster assembly pathway in Arabidopsis

Crystal structure of a prokaryotic (6-4) photolyase with an Fe-S cluster and a 6,7-dimethyl-8-ribityllumazine antenna chromophore

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