A Bridging [4Fe-4S] Cluster and Nucleotide Binding Are Essential for Function of the Cfd1-Nbp35 Complex as a Scaffold in Iron-Sulfur Protein Maturation

Netz, Daili J. A.; Pierik, Antonio J.; Stümpfig, Martin; Bill, Eckhard; Sharma, Anil Kumar; Pallesen, Leif J.; Walden, William E.; Lill, Roland

doi:10.1074/jbc.m111.328914

Cited by 96 publications

(132 citation statements)

References 58 publications

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“…Because of its labile nature, the C-terminal cluster is probably the cluster that is transferred to target apoproteins. The presence of a nucleotide binding domain indicates that NBP35 function needs ATP or GTP, most probably for loading of the Fe-S cluster on the scaffold, as shown in yeast [47]. In fungi and metazoa NBP35 forms a heterotetramer with Cfd1/NUBP1.…”

Section: Discussionmentioning

confidence: 99%

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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Section: Discussionmentioning

confidence: 99%

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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“…Cfd1 and Nbp35 are P-loop NTPases that are thought to function as scaffolds for the initial assembly of FeS clusters in the CIA pathway (13,14). These homologous proteins are members of the ApbC/Nbp35 subfamily of P-loop NTPases that is characterized by a conserved C-terminal ENMS sequence followed by a CX 2 C cysteine cluster (15,16).…”

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confidence: 99%

“…These homologous proteins are members of the ApbC/Nbp35 subfamily of P-loop NTPases that is characterized by a conserved C-terminal ENMS sequence followed by a CX 2 C cysteine cluster (15,16). This C-terminal cysteine cluster confers the ability onto these proteins of binding a bridging [4Fe-4S] cluster between monomers and is essential for activity of both proteins (6,14). Nbp35 also has a cysteine cluster at the N terminus, a feature that distinguishes it from Cfd1 and allows the Nbp35 monomer to bind an additional [4Fe-4S] cluster (7,14).…”

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confidence: 99%

“…This C-terminal cysteine cluster confers the ability onto these proteins of binding a bridging [4Fe-4S] cluster between monomers and is essential for activity of both proteins (6,14). Nbp35 also has a cysteine cluster at the N terminus, a feature that distinguishes it from Cfd1 and allows the Nbp35 monomer to bind an additional [4Fe-4S] cluster (7,14). Cfd1 and Nbp35 form a heterotetrameric complex that upon cluster reconstitution in vitro binds up to four [4Fe-4S] clusters, two clusters bridging monomers, and one cluster coordinated at the N terminus of each Nbp35 monomer (14).…”

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confidence: 99%

“…Nbp35 also has a cysteine cluster at the N terminus, a feature that distinguishes it from Cfd1 and allows the Nbp35 monomer to bind an additional [4Fe-4S] cluster (7,14). Cfd1 and Nbp35 form a heterotetrameric complex that upon cluster reconstitution in vitro binds up to four [4Fe-4S] clusters, two clusters bridging monomers, and one cluster coordinated at the N terminus of each Nbp35 monomer (14). It is currently unknown whether the bridging clusters are between a homodimer or heterodimer within the heterotetrameric arrangement.…”

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confidence: 99%

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Interaction with Cfd1 Increases the Kinetic Lability of FeS on the Nbp35 Scaffold

Pallesen¹,

Solodovnikova²,

Sharma³

et al. 2013

Journal of Biological Chemistry

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Background: A Cfd1 and Nbp35 heterocomplex serves as scaffold for cytosolic iron-sulfur cluster assembly. Results: Deficiency in Cfd1-Nbp35 interaction impaired iron turnover on Nbp35. Conclusion: Cfd1 promotes binding and transfer of labile iron-sulfur cluster on the Nbp35 scaffold. Significance: This is the first insight into the unique roles of these P-loop ATPases in cytosolic iron-sulfur cluster assembly.

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The Nbp35/ApbC homolog acts as a nonessential [4Fe‐4S] transfer protein in methanogenic archaea

et al. 2019

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The nucleotide binding protein 35 (Nbp35)/cytosolic Fe‐S cluster deficient 1 (Cfd1)/alternative pyrimidine biosynthetic protein C (ApbC) protein homologs have been identified in all three domains of life. In eukaryotes, the Nbp35/Cfd1 heterocomplex is an essential Fe‐S cluster assembly scaffold required for the maturation of Fe‐S proteins in the cytosol and nucleus, whereas the bacterial ApbC is an Fe‐S cluster transfer protein only involved in the maturation of a specific target protein. Here, we show that the Nbp35/ApbC homolog MMP0704 purified from its native archaeal host Methanococcus maripaludis contains a [4Fe‐4S] cluster that can be transferred to a [4Fe‐4S] apoprotein. Deletion of mmp0704 from M. maripaludis does not cause growth deficiency under our tested conditions. Our data indicate that Nbp35/ApbC is a nonessential [4Fe‐4S] cluster transfer protein in methanogenic archaea.

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A Bridging [4Fe-4S] Cluster and Nucleotide Binding Are Essential for Function of the Cfd1-Nbp35 Complex as a Scaffold in Iron-Sulfur Protein Maturation

Cited by 96 publications

References 58 publications

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

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

Interaction with Cfd1 Increases the Kinetic Lability of FeS on the Nbp35 Scaffold

The Nbp35/ApbC homolog acts as a nonessential [4Fe‐4S] transfer protein in methanogenic archaea

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