Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co‐chaperone proteins

Maio, Nunziata; Rouault, Tracey A.

doi:10.1002/iub.2593

Cited by 13 publications

(12 citation statements)

References 147 publications

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“…Release of sulfur atoms from cysteine, and ligation to ISCU is promoted by transient binding of frataxin. Sulfur combines with 2 Fe 2+ atoms and 2 reducing equivalents to form a [2Fe-2S] cluster on ISCU [56,57]. The iron necessary for cluster formation originates from an incompletely characterized pool of available iron sometimes referred to as the "chelatable or labile iron pool" [58,59].…”

Section: Fes Cluster Structure Geometries and Biogenesismentioning

confidence: 99%

Regulatory and Sensing Iron-Sulfur Clusters: New Insights and Unanswered Questions

SantaMaria,

Rouault

2024

Preprint

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Iron is an essential nutrient and necessary for biological functions from DNA replication and repair to transcriptional regulation, mitochondrial respiration, electron transfer, oxygen transport, photosynthesis, enzymatic catalysis, and nitrogen fixation. However, due to iron’s propensity to generate toxic radicals which can cause damage to DNA, proteins, and lipids, multiple processes regulate uptake and distribution of iron in living systems. Understanding how intracellular iron metabolism is optimized and how iron is utilized to regulate other intracellular processes is important to our overall understanding of a multitude of biological processes. One of the tools that the cell utilizes to regulate a multitude of functions is ligation of the iron-sulfur (Fe-S) cluster cofactor. Fe-S clusters comprised of iron and inorganic sulfur are ancient components of living matter on earth that are integral for physiological function in all domains of life. Here we will explore the ways in which the cell utilizes Fe-S clusters to sense the intracellular environment and respond to maintain equilibrium.

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Section: Fes Cluster Structure Geometries and Biogenesismentioning

confidence: 99%

Regulatory and Sensing Iron-Sulfur Clusters: New Insights and Unanswered Questions

SantaMaria,

Rouault

2024

Preprint

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“…The release of sulfur atoms from cysteine and ligation to ISCU are promoted by the transient binding of frataxin. Sulfur combines with two Fe 2+ atoms and two reducing equivalents to form a [2Fe-2S] cluster on ISCU [61,62]. The iron necessary for cluster formation originates from an incompletely characterized pool of available iron, sometimes referred to as the "chelatable or labile iron pool" [63,64].…”

Section: Fes Cluster Structure Geometries and Biogenesismentioning

confidence: 99%

Regulatory and Sensing Iron–Sulfur Clusters: New Insights and Unanswered Questions

SantaMaria,

Rouault

2024

Inorganics

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Iron is an essential nutrient and necessary for biological functions from DNA replication and repair to transcriptional regulation, mitochondrial respiration, electron transfer, oxygen transport, photosynthesis, enzymatic catalysis, and nitrogen fixation. However, due to iron’s propensity to generate toxic radicals which can cause damage to DNA, proteins, and lipids, multiple processes regulate the uptake and distribution of iron in living systems. Understanding how intracellular iron metabolism is optimized and how iron is utilized to regulate other intracellular processes is important to our overall understanding of a multitude of biological processes. One of the tools that the cell utilizes to regulate a multitude of functions is the ligation of the iron–sulfur (Fe-S) cluster cofactor. Fe-S clusters comprised of iron and inorganic sulfur are ancient components of living matter on earth that are integral for physiological function in all domains of life. FeS clusters that function as biological sensors have been implicated in a diverse group of life from mammals to bacteria, fungi, plants, and archaea. Here, we will explore the ways in which cells and organisms utilize Fe-S clusters to sense changes in their intracellular environment and restore equilibrium.

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“…Introducing these machineries in the host could be a solution to overcome this issue; however, they are complex machineries involving numerous factors and certain aspects of the Fe-S protein biogenesis remain unclear. 7 , 9 Consequently, several Fe-S proteins have been expressed and purified from E. coli with zinc in their cluster binding sites (e.g. DNA polymerases and the scaffold protein ISCU 112–115 ).…”

Section: Challenges Faced In the De Novo Identific...mentioning

confidence: 99%

“…These protein machineries termed iron sulfur cluster (ISC), sulfur mobilization (SUF), and nitrogen fixation systems have been extensively described in the literature. 7–9 Once the cofactors are formed, they are then secured within proteins via the coordination of the Fe ions to the side chain of surrounding amino acids with cysteine being the most common (all Fe-S clusters are coordinated by at least one cysteine). In this review, the term “ligand” refers to the chemical structure that coordinates the Fe-S cluster, i.e.…”

Section: Introductionmentioning

confidence: 99%

Iron-sulfur protein odyssey: exploring their cluster functional versatility and challenging identification

Vallières,

Benoit,

Guittet

et al. 2024

Metallomics

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Iron-sulfur (Fe-S) clusters are an essential and ubiquitous class of protein-bound prosthetic centers that are involved in a broad range of biological processes (e.g. respiration, photosynthesis, DNA replication and repair and gene regulation) performing a wide range of functions including electron transfer, enzyme catalysis, and sensing. In a general manner, Fe-S clusters can gain or lose electrons through redox reactions, and are highly sensitive to oxidation, notably by small molecules such as oxygen and nitric oxide. The [2Fe-2S] and [4Fe-4S] clusters, the most common Fe-S cofactors, are typically coordinated by four amino acid side chains from the protein, usually cysteine thiolates, but other residues (e.g. histidine, aspartic acid) can be found. While diversity in cluster coordination ensures the functional variety of the Fe-S clusters, the lack of conserved motifs makes new Fe-S protein identification challenging especially when the Fe-S cluster is also shared between two proteins as observed in several dimeric transcriptional regulators and in the mitoribosome. Thanks to the recent development of in cellulo, in vitro and in silico approaches, new Fe-S proteins are still regularly identified, highlighting the functional diversity of this class of proteins. In this review, we will present three main functions of the Fe-S clusters and explain the difficulties encountered to identify Fe-S proteins and methods that have been employed to overcome these issues.

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Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co‐chaperone proteins

Abstract: How to cite this article: Maio N, Rouault TA. Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and cochaperone proteins.

Cited by 13 publications

References 147 publications

Regulatory and Sensing Iron-Sulfur Clusters: New Insights and Unanswered Questions

Regulatory and Sensing Iron-Sulfur Clusters: New Insights and Unanswered Questions

Regulatory and Sensing Iron–Sulfur Clusters: New Insights and Unanswered Questions

Iron-sulfur protein odyssey: exploring their cluster functional versatility and challenging identification

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