Function and crystal structure of the dimeric P-loop ATPase CFD1 coordinating an exposed [4Fe-4S] cluster for transfer to apoproteins

Stehling, Oliver; Jeoung, Jae‐Hun; Freibert, Sven‐Andreas; Paul, Viktoria Désirée; Bänfer, Sebastian; Niggemeyer, Brigitte; Rösser, Ralf; Dobbek, Holger; Lill, Roland

doi:10.1073/pnas.1807762115

Cited by 29 publications

(31 citation statements)

References 82 publications

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“…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. This complex comprises two P-loop NTPases CFD1 and NBP35 ( Roy et al, 2003 ; Hausmann et al, 2005 ; Netz et al, 2007 ; Stehling et al, 2018 ). CFD1 interact with NBP35 and form a heterotetrameric complex.…”

Section: Biogenesis Of Cytosolic and Nuclear Iron–sulfur (Fe/s) Clustersmentioning

confidence: 99%

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

Shi

Hou

Wang

et al. 2021

Front. Cell Dev. Biol.

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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.

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Section: Biogenesis Of Cytosolic and Nuclear Iron–sulfur (Fe/s) Clustersmentioning

confidence: 99%

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

Shi

Hou

Wang

et al. 2021

Front. Cell Dev. Biol.

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“…This is a multistage process consisting of at least two stages: the nascent cluster assembly upon the scaffold complex and delivery to apo-protein [ 76 ]. The scaffold complex consists of NUBP1–NUBP2 protein [ 45 , 77 ] ( Figure 5 ). Such a complex has the ability to bind two [4Fe–4S] clusters on one NUBP1 monomer [ 78 ].…”

Section: Cytosolic Iron–sulfur Cluster Synthesismentioning

confidence: 99%

“…Such a complex has the ability to bind two [4Fe–4S] clusters on one NUBP1 monomer [ 78 ]. The assembly process requires electrons, which are provided by diflavin oxidoreductase (NDOR1) in cooperation with amorosin from NADPH [ 77 , 79 ] ( Figure 5 ). A recent observation describes an interaction between the mitochondrial and cytosolic Fe–S protein assembly machinery linked by NEET proteins (mitoNEET) in which the Fe–S cluster is coordinated by three Cys residues and one His residue [ 80 ].…”

Section: Cytosolic Iron–sulfur Cluster Synthesismentioning

confidence: 99%

“…Transport and insertion into apo-protein of the fully assembled cytosolic Fe–S cluster are supported by the Fe–S protein named CIAO3 (human cytosolic iron–sulfur assembly component 3, also called IOP1) [ 86 , 87 ], in cooperation with the CIA-targeting complex (CTC) [ 77 ]. CTC is composed of the “transducing-like” protein CIAO1 [ 88 ], CIAO2B/FAM96B [ 77 ], and protein MMS19 [ 89 ]. The proteins involved in the CTC complex affect its ability to attach the Fe–S protein and provide stability to this complex [ 90 ].…”

Section: Cytosolic Iron–sulfur Cluster Synthesismentioning

confidence: 99%

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Sulfur Administration in Fe–S Cluster Homeostasis

2021

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Mitochondria are the key organelles of Fe–S cluster synthesis. They contain the enzyme cysteine desulfurase, a scaffold protein, iron and electron donors, and specific chaperons all required for the formation of Fe–S clusters. The newly formed cluster can be utilized by mitochondrial Fe–S protein synthesis or undergo further transformation. Mitochondrial Fe–S cluster biogenesis components are required in the cytosolic iron–sulfur cluster assembly machinery for cytosolic and nuclear cluster supplies. Clusters that are the key components of Fe–S proteins are vulnerable and prone to degradation whenever exposed to oxidative stress. However, once degraded, the Fe–S cluster can be resynthesized or repaired. It has been proposed that sulfurtransferases, rhodanese, and 3-mercaptopyruvate sulfurtransferase, responsible for sulfur transfer from donor to nucleophilic acceptor, are involved in the Fe–S cluster formation, maturation, or reconstitution. In the present paper, we attempt to sum up our knowledge on the involvement of sulfurtransferases not only in sulfur administration but also in the Fe–S cluster formation in mammals and yeasts, and on reconstitution-damaged cluster or restoration of enzyme’s attenuated activity.

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“…The CIA machinery is composed of up to 13 known proteins that assemble both cytosolic and nuclear Fe-S proteins. Initially, a [4Fe-4S] cluster is assembled on the CIA scaffold complex formed between CFD1-NBP35 (Figure 9) [125,126]. The initial cluster synthesis on CFD1-NBP35 further requires the electron transfer chain composed of the flavin-dependent oxidoreductase NDOR1 and CIAPIN1, however, the precise role of the electron-transfer for cluster synthesis is not completely understood yet [127,128].…”

Section: Cytosolic Fe-s Cluster Assembly: the Cia Machinerymentioning

confidence: 99%

The Requirement of Inorganic Fe-S Clusters for the Biosynthesis of the Organometallic Molybdenum Cofactor

et al. 2020

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Iron-sulfur (Fe-S) clusters are essential protein cofactors. In enzymes, they are present either in the rhombic [2Fe-2S] or the cubic [4Fe-4S] form, where they are involved in catalysis and electron transfer and in the biosynthesis of metal-containing prosthetic groups like the molybdenum cofactor (Moco). Here, we give an overview of the assembly of Fe-S clusters in bacteria and humans and present their connection to the Moco biosynthesis pathway. In all organisms, Fe-S cluster assembly starts with the abstraction of sulfur from l-cysteine and its transfer to a scaffold protein. After formation, Fe-S clusters are transferred to carrier proteins that insert them into recipient apo-proteins. In eukaryotes like humans and plants, Fe-S cluster assembly takes place both in mitochondria and in the cytosol. Both Moco biosynthesis and Fe-S cluster assembly are highly conserved among all kingdoms of life. Moco is a tricyclic pterin compound with molybdenum coordinated through its unique dithiolene group. Moco biosynthesis begins in the mitochondria in a Fe-S cluster dependent step involving radical/S-adenosylmethionine (SAM) chemistry. An intermediate is transferred to the cytosol where the dithiolene group is formed, to which molybdenum is finally added. Further connections between Fe-S cluster assembly and Moco biosynthesis are discussed in detail.

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Function and crystal structure of the dimeric P-loop ATPase CFD1 coordinating an exposed [4Fe-4S] cluster for transfer to apoproteins

Cited by 29 publications

References 82 publications

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

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

Sulfur Administration in Fe–S Cluster Homeostasis

The Requirement of Inorganic Fe-S Clusters for the Biosynthesis of the Organometallic Molybdenum Cofactor

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