Frataxin Structure and Function

Castro, Ignacio Hugo; Pignataro, María Florencia; Sewell, Karl Ellioth; Espeche, Lucía D.; Herrera, María Georgina; Noguera, Martín Ezequiel; Daín, Liliana; Nadra, Alejandro D.; Arán, Martı́n; Smal, Clara; Gallo, Mariana; Santos, Javier

doi:10.1007/978-3-030-28151-9_13

Cited by 22 publications

(21 citation statements)

References 105 publications

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“…The human proteins of the iron-sulfur cluster (ISC) assembly machinery are all soluble proteins located in the mitochondrial matrix [63]. De novo Fe-S cluster synthesis occurs on the mitochondrial scaffold protein ISCU and requires a high molecular weight complex composed of five proteins: frataxin, a protein for which several functions have been proposed [64][65][66][67][68][69][70], the enzyme cysteine desulfurase NFS1, the small factors ISD11 and acyl carrier protein (ACP), and ISCU [71,72]. In vivo data [73] showed that the second step of the human ISC assembly process is the transfer of the newly synthetized cluster to the mitochondrial monothiol glutaredoxin, GLRX5, which acts as a [2Fe-2S] cluster transfer protein.…”

Section: Iron-sulfur Proteins: From Electron Transfer To Cluster Biogmentioning

confidence: 99%

Paramagnetic NMR Spectroscopy Is a Tool to Address Reactivity, Structure, and Protein–Protein Interactions of Metalloproteins: The Case of Iron–Sulfur Proteins

Piccioli¹

2020

Magnetochemistry

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The study of cellular machineries responsible for the iron–sulfur (Fe–S) cluster biogenesis has led to the identification of a large number of proteins, whose importance for life is documented by an increasing number of diseases linked to them. The labile nature of Fe–S clusters and the transient protein–protein interactions, occurring during the various steps of the maturation process, make their structural characterization in solution particularly difficult. Paramagnetic nuclear magnetic resonance (NMR) has been used for decades to characterize chemical composition, magnetic coupling, and the electronic structure of Fe–S clusters in proteins; it represents, therefore, a powerful tool to study the protein–protein interaction networks of proteins involving into iron–sulfur cluster biogenesis. The optimization of the various NMR experiments with respect to the hyperfine interaction will be summarized here in the form of a protocol; recently developed experiments for measuring longitudinal and transverse nuclear relaxation rates in highly paramagnetic systems will be also reviewed. Finally, we will address the use of extrinsic paramagnetic centers covalently bound to diamagnetic proteins, which contributed over the last twenty years to promote the applications of paramagnetic NMR well beyond the structural biology of metalloproteins.

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Section: Iron-sulfur Proteins: From Electron Transfer To Cluster Biogmentioning

confidence: 99%

Paramagnetic NMR Spectroscopy Is a Tool to Address Reactivity, Structure, and Protein–Protein Interactions of Metalloproteins: The Case of Iron–Sulfur Proteins

Piccioli¹

2020

Magnetochemistry

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“…Most of the newly identified proteins are associated with the small subunit and distributed across the head and the two regions that we named as the back protuberance and the body extension. These include SelR, a methionine-R-sulfoxide reductase ( Kryukov et al, 2002 ) in the body extension, mS81 and an apo-frataxin protein ( Castro et al, 2019 ) in the back protuberance, mS86. In the large mitoribosomal subunit (LSU), we identified a protein binding two iron-sulfur clusters via CDGSH motifs ( Sengupta et al, 2018 ), mL107.…”

Section: Resultsmentioning

confidence: 99%

Ciliate mitoribosome illuminates evolutionary steps of mitochondrial translation

Tobiasson

Amunts

2020

eLife

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To understand the steps involved in the evolution of translation, we used Tetrahymena thermophila, a ciliate with high coding capacity of the mitochondrial genome, as the model organism and characterized its mitochondrial ribosome (mitoribosome) using cryo-EM. The structure of the mitoribosome reveals an assembly of 94-ribosomal proteins and four-rRNAs with an additional protein mass of ~700 kDa on the small subunit, while the large subunit lacks 5S rRNA. The structure also shows that the small subunit head is constrained, tRNA binding sites are formed by mitochondria-specific protein elements, conserved protein bS1 is excluded, and bacterial RNA polymerase binding site is blocked. We provide evidence for anintrinsic protein targeting system through visualization of mitochondria-specific mL105 by the exit tunnel that would facilitate the recruitment of a nascent polypeptide. Functional protein uS3m is encoded by three complementary genes from the nucleus and mitochondrion, establishing a link between genetic drift and mitochondrial translation. Finally, we reannotated nine open reading frames in the mitochondrial genome that code for mitoribosomal proteins.

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“…Three genes encoding ISU1-3 were found in Arabidopsis (At4g22220, At3g01020, At4g04080) [ 31 , 38 , 39 ], while ACP is an acyl group carrier protein, homologous to Arabidopsis AtACP1-3 [ 40 ]. Finally, frataxin is a highly conserved protein from prokaryotes to eukaryotes [ 41 , 42 ]. This protein has been involved in various processes such as Fe homeostasis, respiration, heme metabolism, oxidative stress, and transfer of persulfide groups [ 43 , 44 , 45 , 46 , 47 , 48 , 49 ].…”

Section: Synthesis Of Fe-s Clustersmentioning

confidence: 99%

Fe-S Protein Synthesis in Green Algae Mitochondria

Gómez-Casati

Busi

Barchiesi

et al. 2021

Plants

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Iron and sulfur are two essential elements for all organisms. These elements form the Fe-S clusters that are present as cofactors in numerous proteins and protein complexes related to key processes in cells, such as respiration and photosynthesis, and participate in numerous enzymatic reactions. In photosynthetic organisms, the ISC and SUF Fe-S cluster synthesis pathways are located in organelles, mitochondria, and chloroplasts, respectively. There is also a third biosynthetic machinery in the cytosol (CIA) that is dependent on the mitochondria for its function. The genes and proteins that participate in these assembly pathways have been described mainly in bacteria, yeasts, humans, and recently in higher plants. However, little is known about the proteins that participate in these processes in algae. This review work is mainly focused on releasing the information on the existence of genes and proteins of green algae (chlorophytes) that could participate in the assembly process of Fe-S groups, especially in the mitochondrial ISC and CIA pathways.

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Frataxin Structure and Function

Cited by 22 publications

References 105 publications

Paramagnetic NMR Spectroscopy Is a Tool to Address Reactivity, Structure, and Protein–Protein Interactions of Metalloproteins: The Case of Iron–Sulfur Proteins

Paramagnetic NMR Spectroscopy Is a Tool to Address Reactivity, Structure, and Protein–Protein Interactions of Metalloproteins: The Case of Iron–Sulfur Proteins

Ciliate mitoribosome illuminates evolutionary steps of mitochondrial translation

Fe-S Protein Synthesis in Green Algae Mitochondria

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