Search results for: Simone Ciofi-Baffoni

Items from 1 to 20 out of 30 results

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Unraveling the mechanism of [4Fe‐4S] cluster assembly on the N‐terminal cluster binding site of NUBP1

Beatrice Bargagna, Sara Matteucci, Simone Ciofi‐Baffoni, Francesca Camponeschi, more

[4Fe‐4S]²⁺ cluster assembly in human cytosol requires both a [2Fe‐2S] cluster chaperone being able to donate two [2Fe‐2S]²⁺ clusters and an electron donor providing two electrons to reductively couple the two [2Fe‐2S]²⁺ clusters into a [4Fe‐4S]²⁺ cluster. The mechanism through which the cytosolic [4Fe‐4S]²⁺ cluster assembly works is still not defined. Here, we show that a hetero‐tetrameric complex...

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In Cellulo Mössbauer and EPR Studies Bring New Evidence to the Long‐Standing Debate on Iron–Sulfur Cluster Binding in Human Anamorsin

Sara Matteucci, Francesca Camponeschi, Martin Clémancey, Simone Ciofi‐Baffoni, more

Angewandte Chemie > 133 > 27 > 14967 - 14971

Human anamorsin is an iron–sulfur (Fe–S)‐cluster‐binding protein acting as an electron donor in the early steps of cytosolic iron–sulfur protein biogenesis. Human anamorsin belongs to the eukaryotic CIAPIN1 protein family and contains two highly conserved cysteine‐rich motifs, each binding an Fe–S cluster. In vitro works by various groups have provided rather controversial results for the type of...

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In Cellulo Mössbauer and EPR Studies Bring New Evidence to the Long‐Standing Debate on Iron–Sulfur Cluster Binding in Human Anamorsin

Sara Matteucci, Francesca Camponeschi, Martin Clémancey, Simone Ciofi‐Baffoni, more

Angewandte Chemie International Edition > 60 > 27 > 14841 - 14845

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A pathway for assembling [4Fe‐4S]²⁺ clusters in mitochondrial iron–sulfur protein biogenesis

Veronica Nasta, Dafne Suraci, Spyridon Gourdoupis, Simone Ciofi‐Baffoni, more

The FEBS Journal > 287 > 11 > 2312 - 2327

During its late steps, the mitochondrial iron–sulfur cluster (ISC) assembly machinery leads to the formation of [4Fe‐4S] clusters. In vivo studies revealed that several proteins are implicated in the biosynthesis and trafficking of [4Fe‐4S] clusters in mitochondria. However, they do not provide a clear picture into how these proteins cooperate. Here, we showed that three late‐acting components of...

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Correction to: The NMR contribution to protein–protein networking in Fe–S protein maturation

Lucia Banci, Francesca Camponeschi, Simone Ciofi‑Baffoni, Mario Piccioli

JBIC Journal of Biological Inorganic Chemistry > 2018 > 23 > 4 > 687-687

The article “The NMR contribution to protein–protein networking in Fe–S protein maturation”, written by Lucia Banci, Francesca Camponeschi, Simone Ciofi‑Baffoni, Mario Piccioli was originally published electronically on the publisher’s internet portal (currently SpringerLink) on 22 March, 2018 without open access.

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The NMR contribution to protein–protein networking in Fe–S protein maturation

Lucia Banci, Francesca Camponeschi, Simone Ciofi-Baffoni, Mario Piccioli

JBIC Journal of Biological Inorganic Chemistry > 2018 > 23 > 4 > 665-685

Iron–sulfur proteins were among the first class of metalloproteins that were actively studied using NMR spectroscopy tailored to paramagnetic systems. The hyperfine shifts, their temperature dependencies and the relaxation rates of nuclei of cluster-bound residues are an efficient fingerprint of the nature and the oxidation state of the Fe–S cluster. NMR significantly contributed to the analysis of...

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Structural insights into the molecular function of human [2Fe-2S] BOLA1-GRX5 and [2Fe-2S] BOLA3-GRX5 complexes

Veronica Nasta, Andrea Giachetti, Simone Ciofi-Baffoni, Lucia Banci

Biochimica et Biophysica Acta (BBA) - General Subjects > 2017 > 1861 > 8 > 2119-2131

Members of the monothiol glutaredoxin family and members of the BolA-like protein family have recently emerged as specific interacting partners involved in iron-sulfur protein maturation and redox regulation pathways. It is known that human mitochondrial BOLA1 and BOLA3 form [2Fe-2S] cluster-bridged dimeric heterocomplexes with the monothiol glutaredoxin GRX5. The structure and cluster coordination...

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The IR-¹⁵N-HSQC-AP experiment: a new tool for NMR spectroscopy of paramagnetic molecules

Simone Ciofi-Baffoni, Angelo Gallo, Riccardo Muzzioli, Mario Piccioli

Journal of Biomolecular NMR > 2014 > 58 > 2 > 123-128

A crucial factor for the understanding of structure-function relationships in metalloproteins is the identification of NMR signals from residues surrounding the metal cofactor. When the latter is paramagnetic, the NMR information in the proximity of the metal center may be scarce, because fast nuclear relaxation quenches signal intensity and coherence transfer efficiency. To identify residues at a...

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An Intrinsically Disordered Domain Has a Dual Function Coupled to Compartment-Dependent Redox Control

Lucia Banci, Ivano Bertini, Chiara Cefaro, Simone Ciofi-Baffoni, more

Journal of Molecular Biology > 2013 > 425 > 3 > 594-608

The functional role of unstructured protein domains is an emerging field in the frame of intrinsically disordered proteins. The involvement of intrinsically disordered domains (IDDs) in protein targeting and biogenesis processes in mitochondria is so far not known. Here, we have characterized the structural/dynamic and functional properties of an IDD of the sulfhydryl oxidase ALR (augmenter of liver...

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Human anamorsin binds [2Fe–2S] clusters with unique electronic properties

Lucia Banci, Simone Ciofi-Baffoni, Maciej Mikolajczyk, Julia Winkelmann, more

JBIC Journal of Biological Inorganic Chemistry > 2013 > 18 > 8 > 883-893

The eukaryotic anamorsin protein family, which has recently been proposed to be part of an electron transfer chain functioning in the early steps of cytosolic iron–sulfur (Fe/S) protein biogenesis, is characterized by a largely unstructured domain (CIAPIN1) containing two conserved cysteine-rich motifs (CX₈CX₂CXC and CX₂CX₇CX₂C) whose Fe/S binding properties and electronic structures are not well...

article

Structural characterization of CHCHD5 and CHCHD7: Two atypical human twin CX9C proteins

Lucia Banci, Ivano Bertini, Simone Ciofi-Baffoni, Deepa Jaiswal, more

Journal of Structural Biology > 2012 > 180 > 1 > 190-200

Twin CX ₉ C proteins constitute a large protein family among all eukaryotes; are putative substrates of the mitochondrial Mia40-dependent import machinery; contain a coiled coil-helix-coiled coil-helix (CHCH) fold stabilized by two disulfide bonds as exemplified by three structures available for this family. However, they considerably differ at the primary sequence level and this prevents...

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Copper exposure effects on yeast mitochondrial proteome

Lucia Banci, Ivano Bertini, Simone Ciofi-Baffoni, Annamaria D'Alessandro, more

Journal of Proteomics > 2011 > 74 > 11 > 2522-2535

Mitochondria play an important role on the entire cellular copper homeostatic mechanisms. Alteration of cellular copper levels may thus influence mitochondrial proteome and its investigation represents an important contribution to the general understanding of copper-related cellular effects. In these study we have performed an organelle targeted proteomic investigation focusing our attention on the...

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Anamorsin Is a [2Fe-2S] Cluster-Containing Substrate of the Mia40-Dependent Mitochondrial Protein Trapping Machinery

Lucia Banci, Ivano Bertini, Simone Ciofi-Baffoni, Francesca Boscaro, more

Chemistry & Biology > 2011 > 18 > 6 > 794-804

Human anamorsin was implicated in cytosolic iron-sulfur (Fe/S) protein biogenesis. Here, the structural and metal-binding properties of anamorsin and its interaction with Mia40, a well-known oxidoreductase involved in protein trapping in the mitochondrial intermembrane space (IMS), were characterized. We show that (1), anamorsin contains two structurally independent domains connected by an unfolded...

article

Seeking the determinants of the elusive functions of Sco proteins

Lucia Banci, Ivano Bertini, Gabriele Cavallaro, Simone Ciofi‐Baffoni

The FEBS Journal > 278 > 13 > 2244 - 2262

Sco proteins are present in all types of organisms, including the vast majority of eukaryotes and many prokaryotes. It is well established that Sco proteins in eukaryotes are involved in the assembly of the Cu_A cofactor of mitochondrial cytochrome c oxidase; however their precise role in this process has not yet been elucidated at the molecular level. In particular, some but not all eukaryotes including...

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Sco proteins are involved in electron transfer processes

Lucia Banci, Ivano Bertini, Simone Ciofi-Baffoni, Tatiana Kozyreva, more

JBIC Journal of Biological Inorganic Chemistry > 2011 > 16 > 3 > 391-403

Sco proteins are widespread in eukaryotic and in many prokaryotic organisms. They have a thioredoxin-like fold and bind a single copper(I) or copper(II) ion through a CXXXC motif and a conserved His ligand, with both tight and weak affinities. They have been implicated in the assembly of the Cu_A site of cytochrome c oxidase as copper chaperones and/or thioredoxins. In this work we have structurally...

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Cellular copper distribution: a mechanistic systems biology approach

Lucia Banci, Ivano Bertini, Francesca Cantini, Simone Ciofi-Baffoni

Cellular and Molecular Life Sciences > 2010 > 67 > 15 > 2563-2589

Copper is an essential but potentially harmful trace element required in many enzymatic processes involving redox chemistry. Cellular copper homeostasis in mammals is predominantly maintained by regulating copper transport through the copper import CTR proteins and the copper exporters ATP7A and ATP7B. Once copper is imported into the cell, several pathways involving a number of copper proteins are...

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NMR structural analysis of the soluble domain of ZiaA-ATPase and the basis of selective interactions with copper metallochaperone Atx1

Lucia Banci, Ivano Bertini, Simone Ciofi-Baffoni, Luisa Poggi, more

JBIC Journal of Biological Inorganic Chemistry > 2010 > 15 > 1 > 87-98

A Cu(I) metallochaperone, Atx1, interacts with the amino-terminal domain of a Cu(I)-transporting ATPase, PacS_N, but not with a domain of related Zn-transporting ATPase, ZiaA_N in Synechocystis PCC 6803. This is thought to prevent ZiaA_N from acquiring Cu(I), which it binds more tightly than Zn. Solution structures of Atx1, PacS_N, and the heterodimer were previously described. Here we report solution...

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The coiled coil-helix-coiled coil-helix proteins may be redox proteins

Lucia Banci, Ivano Bertini, Simone Ciofi-Baffoni, Kostas Tokatlidis

FEBS Letters > 2009 > 583 > 11 > 1699-1702

A number of nuclear encoded proteins are imported in to the intermembrane space of mitochondria where they adopt a coiled coil-helix-coiled coil-helix (CHCH) fold. Two disulfide bonds formed by twin CX ₃ C or CX ₉ C motifs stabilize this fold. Some of these proteins are also characterized at their N-termini by the presence of two additional cysteine residues which can perform oxidoreductase...

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A Structural Characterization of Human SCO2

Lucia Banci, Ivano Bertini, Simone Ciofi-Baffoni, Ioannis P. Gerothanassis, more

Structure > 2007 > 15 > 9 > 1132-1140

Human Sco2 is a mitochondrial membrane-bound protein involved in copper supply for the assembly of cytochrome c oxidase in eukaryotes. Its precise action is not yet understood. We report here a structural and dynamic characterization by NMR of the apo and copper(I) forms of the soluble fragment. The structural and metal binding features of human Cu(I)Sco2 are similar to the more often studied Sco1...

article

Modeling Protein−Protein Complexes Involved in the Cytochrome c Oxidase Copper-Delivery Pathway

Aalt D. J. van Dijk, Simone Ciofi-Baffoni, Lucia Banci, Ivano Bertini, more

Journal of Proteome Research > 2007 > 6 > 4 > 1530 - 1539

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Search results for: Simone Ciofi-Baffoni

Unraveling the mechanism of [4Fe‐4S] cluster assembly on the N‐terminal cluster binding site of NUBP1

In Cellulo Mössbauer and EPR Studies Bring New Evidence to the Long‐Standing Debate on Iron–Sulfur Cluster Binding in Human Anamorsin

In Cellulo Mössbauer and EPR Studies Bring New Evidence to the Long‐Standing Debate on Iron–Sulfur Cluster Binding in Human Anamorsin

A pathway for assembling [4Fe‐4S]²⁺ clusters in mitochondrial iron–sulfur protein biogenesis

Correction to: The NMR contribution to protein–protein networking in Fe–S protein maturation

The NMR contribution to protein–protein networking in Fe–S protein maturation

Structural insights into the molecular function of human [2Fe-2S] BOLA1-GRX5 and [2Fe-2S] BOLA3-GRX5 complexes

The IR-¹⁵N-HSQC-AP experiment: a new tool for NMR spectroscopy of paramagnetic molecules

An Intrinsically Disordered Domain Has a Dual Function Coupled to Compartment-Dependent Redox Control

Human anamorsin binds [2Fe–2S] clusters with unique electronic properties

Structural characterization of CHCHD5 and CHCHD7: Two atypical human twin CX9C proteins

Copper exposure effects on yeast mitochondrial proteome

Anamorsin Is a [2Fe-2S] Cluster-Containing Substrate of the Mia40-Dependent Mitochondrial Protein Trapping Machinery

Seeking the determinants of the elusive functions of Sco proteins

Sco proteins are involved in electron transfer processes

Cellular copper distribution: a mechanistic systems biology approach

NMR structural analysis of the soluble domain of ZiaA-ATPase and the basis of selective interactions with copper metallochaperone Atx1

The coiled coil-helix-coiled coil-helix proteins may be redox proteins

A Structural Characterization of Human SCO2

Modeling Protein−Protein Complexes Involved in the Cytochrome c Oxidase Copper-Delivery Pathway

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