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

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

doi:10.1007/s00775-018-1573-5

The Yeast Scaffold Proteins Isu1p and Isu2p Are Required inside Mitochondria for Maturation of Cytosolic Fe/S Proteins

Molecular and Cellular Biology ◽

10.1128/mcb.24.11.4848-4857.2004 ◽

2004 ◽

Vol 24 (11) ◽

pp. 4848-4857 ◽

Cited By ~ 94

Author(s):

Jana Gerber ◽

Karina Neumann ◽

Corinna Prohl ◽

Ulrich Mühlenhoff ◽

Roland Lill

Keyword(s):

Iron Homeostasis ◽

De Novo ◽

Mitochondrial Targeting ◽

Protein Maturation ◽

Iron Sulfur Cluster ◽

Subcellular Compartment ◽

S Protein ◽

Iron Sulfur ◽

Protein Biogenesis ◽

S Proteins

ABSTRACT Iron-sulfur (Fe/S) proteins are located in mitochondria, cytosol, and nucleus. Mitochondrial Fe/S proteins are matured by the iron-sulfur cluster (ISC) assembly machinery. Little is known about the formation of Fe/S proteins in the cytosol and nucleus. A function of mitochondria in cytosolic Fe/S protein maturation has been noted, but small amounts of some ISC components have been detected outside mitochondria. Here, we studied the highly conserved yeast proteins Isu1p and Isu2p, which provide a scaffold for Fe/S cluster synthesis. We asked whether the Isu proteins are needed for biosynthesis of cytosolic Fe/S clusters and in which subcellular compartment the Isu proteins are required. The Isu proteins were found to be essential for de novo biosynthesis of both mitochondrial and cytosolic Fe/S proteins. Several lines of evidence indicate that Isu1p and Isu2p have to be located inside mitochondria in order to perform their function in cytosolic Fe/S protein maturation. We were unable to mislocalize Isu1p to the cytosol due to the presence of multiple, independent mitochondrial targeting signals in this protein. Further, the bacterial homologue IscU and the human Isu proteins (partially) complemented the defects of yeast Isu protein-depleted cells in growth rate, Fe/S protein biogenesis, and iron homeostasis, yet only after targeting to mitochondria. Together, our data suggest that the Isu proteins need to be localized in mitochondria to fulfill their functional requirement in Fe/S protein maturation in the cytosol.

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

JBIC Journal of Biological Inorganic Chemistry ◽

10.1007/s00775-018-1552-x ◽

2018 ◽

Vol 23 (4) ◽

pp. 665-685 ◽

Cited By ~ 8

Author(s):

Lucia Banci ◽

Francesca Camponeschi ◽

Simone Ciofi-Baffoni ◽

Mario Piccioli

Keyword(s):

Protein Maturation ◽

S Protein

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Human ABC7 transporter: gene structure and mutation causing X-linked sideroblastic anemia with ataxia with disruption of cytosolic iron-sulfur protein maturation

Blood ◽

10.1182/blood.v96.9.3256.h8003256_3256_3264 ◽

2000 ◽

Vol 96 (9) ◽

pp. 3256-3264 ◽

Cited By ~ 5

Author(s):

Soumeya Bekri ◽

Gyula Kispal ◽

Heike Lange ◽

Edward Fitzsimons ◽

John Tolmie ◽

...

Keyword(s):

Missense Mutation ◽

Transmembrane Domain ◽

Molecular Defect ◽

Protein Maturation ◽

Sideroblastic Anemia ◽

S Protein ◽

Iron Sulfur ◽

Sulfur Protein ◽

Low Efficiency ◽

A Charge

The human protein ABC7 belongs to the adenosine triphosphate-binding cassette transporter superfamily, and its yeast orthologue, Atm1p, plays a central role in the maturation of cytosolic iron-sulfur (Fe/S) cluster-containing proteins. Previously, a missense mutation in the human ABC7 gene was shown to be the defect in members of a family affected with X-linked sideroblastic anemia with cerebellar ataxia (XLSA/A). Here, the promoter region and the intron/exon structure of the human ABC7 gene were characterized, and the function of wild-type and mutant ABC7 in cytosolic Fe/S protein maturation was analyzed. The gene contains 16 exons, all with intron/exon boundaries following the AG/GT rule. A single missense mutation was found in exon 10 of the ABC7gene in 2 affected brothers with XLSA/A. The mutation was a G-to-A transition at nucleotide 1305 of the full-length cDNA, resulting in a charge inversion caused by the substitution of lysine for glutamate at residue 433 C-terminal to the putative sixth transmembrane domain of ABC7. Expression of normal ABC7 almost fully complemented the defect in the maturation of cytosolic Fe/S proteins in a yeast strain in which the ATM1 gene had been deleted (Δatm1 cells). Thus, ABC7 is a functional orthologue of Atm1p. In contrast, the expression of mutated ABC7 (E433K) or Atm1p (D398K) proteins in Δatm1 cells led to a low efficiency of cytosolic Fe/S protein maturation. These data demonstrate that both the molecular defect in XLSA/A and the impaired maturation of a cytosolic Fe/S protein result from an ABC7 mutation in the reported family.

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Monitoring of S Protein Maturation in the Endoplasmic Reticulum by Calnexin Is Important for the Infectivity of Severe Acute Respiratory Syndrome Coronavirus

Journal of Virology ◽

10.1128/jvi.01250-12 ◽

2012 ◽

Vol 86 (21) ◽

pp. 11745-11753 ◽

Cited By ~ 35

Author(s):

M. Fukushi ◽

Y. Yoshinaka ◽

Y. Matsuoka ◽

S. Hatakeyama ◽

Y. Ishizaka ◽

...

Keyword(s):

Endoplasmic Reticulum ◽

Severe Acute Respiratory Syndrome ◽

Protein Maturation ◽

S Protein

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Human ABC7 transporter: gene structure and mutation causing X-linked sideroblastic anemia with ataxia with disruption of cytosolic iron-sulfur protein maturation

Blood ◽

10.1182/blood.v96.9.3256 ◽

2000 ◽

Vol 96 (9) ◽

pp. 3256-3264 ◽

Cited By ~ 180

Author(s):

Soumeya Bekri ◽

Gyula Kispal ◽

Heike Lange ◽

Edward Fitzsimons ◽

John Tolmie ◽

...

Keyword(s):

Missense Mutation ◽

Transmembrane Domain ◽

Molecular Defect ◽

Protein Maturation ◽

Sideroblastic Anemia ◽

S Protein ◽

Iron Sulfur ◽

Sulfur Protein ◽

Low Efficiency ◽

A Charge

Abstract The human protein ABC7 belongs to the adenosine triphosphate-binding cassette transporter superfamily, and its yeast orthologue, Atm1p, plays a central role in the maturation of cytosolic iron-sulfur (Fe/S) cluster-containing proteins. Previously, a missense mutation in the human ABC7 gene was shown to be the defect in members of a family affected with X-linked sideroblastic anemia with cerebellar ataxia (XLSA/A). Here, the promoter region and the intron/exon structure of the human ABC7 gene were characterized, and the function of wild-type and mutant ABC7 in cytosolic Fe/S protein maturation was analyzed. The gene contains 16 exons, all with intron/exon boundaries following the AG/GT rule. A single missense mutation was found in exon 10 of the ABC7gene in 2 affected brothers with XLSA/A. The mutation was a G-to-A transition at nucleotide 1305 of the full-length cDNA, resulting in a charge inversion caused by the substitution of lysine for glutamate at residue 433 C-terminal to the putative sixth transmembrane domain of ABC7. Expression of normal ABC7 almost fully complemented the defect in the maturation of cytosolic Fe/S proteins in a yeast strain in which the ATM1 gene had been deleted (Δatm1 cells). Thus, ABC7 is a functional orthologue of Atm1p. In contrast, the expression of mutated ABC7 (E433K) or Atm1p (D398K) proteins in Δatm1 cells led to a low efficiency of cytosolic Fe/S protein maturation. These data demonstrate that both the molecular defect in XLSA/A and the impaired maturation of a cytosolic Fe/S protein result from an ABC7 mutation in the reported family.

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The mitochondrial carrier Rim2 co-imports pyrimidine nucleotides and iron

Biochemical Journal ◽

10.1042/bj20130144 ◽

2013 ◽

Vol 455 (1) ◽

pp. 57-65 ◽

Cited By ~ 23

Author(s):

Elisabeth M. Froschauer ◽

Nicole Rietzschel ◽

Melanie R. Hassler ◽

Markus Binder ◽

Rudolf J. Schweyen ◽

...

Keyword(s):

Metal Ions ◽

Divalent Metal ◽

Divalent Metal Ions ◽

Protein Maturation ◽

Pyrimidine Nucleotides ◽

Mitochondrial Carrier ◽

S Protein ◽

Pyrimidine Nucleotide ◽

Iron Supply ◽

Mitochondrial Iron

Mitochondrial iron uptake is of key importance both for organelle function and cellular iron homoeostasis. The mitochondrial carrier family members Mrs3 and Mrs4 (homologues of vertebrate mitoferrin) function in organellar iron supply, yet other low efficiency transporters may exist. In Saccharomyces cerevisiae, overexpression of RIM2 (MRS12) encoding a mitochondrial pyrimidine nucleotide transporter can overcome the iron-related phenotypes of strains lacking both MRS3 and MRS4. In the present study we show by in vitro transport studies that Rim2 mediates the transport of iron and other divalent metal ions across the mitochondrial inner membrane in a pyrimidine nucleotide-dependent fashion. Mutations in the proposed substrate-binding site of Rim2 prevent both pyrimidine nucleotide and divalent ion transport. These results document that Rim2 catalyses the co-import of pyrimidine nucleotides and divalent metal ions including ferrous iron. The deletion of RIM2 alone has no significant effect on mitochondrial iron supply, Fe–S protein maturation and haem synthesis. However, RIM2 deletion in mrs3/4Δ cells aggravates their Fe–S protein maturation defect. We conclude that under normal physiological conditions Rim2 does not play a significant role in mitochondrial iron acquisition, yet, in the absence of the main iron transporters Mrs3 and Mrs4, this carrier can supply the mitochondrial matrix with iron in a pyrimidine-nucleotide-dependent fashion.

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A T.E.M. study of mouse mammary epithelial cell secretory differentiation cultured on collagen and Matrigel

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100085241 ◽

1991 ◽

Vol 49 ◽

pp. 188-189

Author(s):

W.N. Bentham ◽

V. Rocha

Keyword(s):

Cell Culture ◽

Mammary Epithelial ◽

Secretory Process ◽

Cell Culture System ◽

Protein Maturation ◽

Cell Culture Techniques ◽

Culture Techniques ◽

Mouse Mammary Epithelial Cell ◽

Secretory Differentiation

It has been an interest of our lab to develop a mammary epethelial cell culture system that faithfully duplicates the in vivo condition of the lactating gland. Since the introduction of collagen as a matrix on which cells are cultivated other E.C.M. type matrices have been made available and are used in many cell culture techniques. We have previously demonstrated that cells cultured on collagen and Matrigel do not differentiate as they do in vivo. It seems that these cultures often produce cells that show a disruption in the secretory process. The appearance of large ribosomal studded vesicles, that specifically label with antibody to casein, suggest an interruption of both protein maturation and secretion at the E.R. to golgi transition. In this report we have examined cultures on collagen and Matrigel at relative high and low seeding densities and compared them to cells from the in vivo condition.

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