Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe–2S] clusters

@article{Bandyopadhyay2008ChloroplastMG,
  title={Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe–2S] clusters},
  author={Sibali Bandyopadhyay and Filipe Gama and María Micaela Molina-Navarro and Jos{\'e} Manuel Gualberto and Ronald Claxton and Sunil G. Naik and Boi Hanh Huynh and Enrique Herrero and Jean-Pierre Jacquot and Michael K. Johnson and Nicolas Rouhier},
  journal={The EMBO Journal},
  year={2008},
  volume={27}
}
Glutaredoxins (Grxs) are small oxidoreductases that reduce disulphide bonds or protein‐glutathione mixed disulphides. More than 30 distinct grx genes are expressed in higher plants, but little is currently known concerning their functional diversity. This study presents biochemical and spectroscopic evidence for incorporation of a [2Fe–2S] cluster in two heterologously expressed chloroplastic Grxs, GrxS14 and GrxS16, and in vitro cysteine desulphurase‐mediated assembly of an identical [2Fe–2S… Expand
The Arabidopsis Mitochondrial Glutaredoxin GRXS15 Provides [2Fe-2S] Clusters for ISCA-Mediated [4Fe-4S] Cluster Maturation
TLDR
A detailed characterization of the interactions between Arabidopsis thaliana GRXS15 and ISCA proteins using both in vivo and in vitro approaches is reported, providing new insights into the roles of GRXs15 andISCA1a/2 in effecting [2Fe-2S]2+ to [4Fe-4S] 2+ cluster conversions for the maturation of client [4 Fe-4s] cluster-containing proteins in plants. Expand
Arabidopsis Chloroplastic Glutaredoxin C5 as a Model to Explore Molecular Determinants for Iron-Sulfur Cluster Binding into Glutaredoxins*
TLDR
Thiol titrations, fluorescence measurements, and mass spectrometry analyses showed that, despite the presence of a dithiol active site, AtGrxC5 does not form any inter- or intramolecular disulfide bond and that its activity exclusively relies on a monothiol mechanism. Expand
Monothiol Glutaredoxins Function in Storing and Transporting [Fe2S2] Clusters Assembled on IscU Scaffold Proteins
TLDR
The results support a role for monothiol Grx’s in storing and transporting [Fe2S2]2+ clusters assembled on IscU and illustrate the limitations of interpreting in vitro cluster transfer studies involving [Fe 2S2]-IscU in the absence of the dedicated HscA/HscB co-chaperone system. Expand
Monothiol CGFS glutaredoxins and BolA-like proteins: [2Fe-2S] binding partners in iron homeostasis.
TLDR
Recent progress in uncovering the cellular and molecular mechanisms by which CGFS Grxs and BolA-like proteins help regulate iron metabolism in both eukaryotic and prokaryotic organisms is reviewed. Expand
Characterization of the human monothiol glutaredoxin 3 (PICOT) as iron-sulfur protein.
TLDR
This work characterized Grx3/PICOT as iron-sulfur protein, and found that redox-induced dissociation of the Grx2-2S-2+ clusters were not redox active, instead they were lost upon treatment of the holo protein with ferricyanide or S-nitroso glutathione. Expand
The function of glutaredoxin GRXS15 is required for lipoyl-dependent dehydrogenases in mitochondria.
TLDR
An in-depth metabolic analysis of the variant and knockdown GRXS15 lines shows that most Fe-S cluster-dependent processes are not affected, and an increase in most TCA cycle intermediates and amino acids, especially pyruvate, glycine and branched-chain amino acids (BCAAs). Expand
Chloroplast HCF101 is a scaffold protein for [4Fe-4S] cluster assembly
TLDR
It is demonstrated that the reconstituted cluster is transiently bound and can be transferred from HCF101 to a [4Fe-4S] apoprotein, and these findings suggest that HCF 101 may serve as a chloroplast scaffold protein that specifically assembles [4 Fe- 4S] clusters and transfers them to thechloroplast membrane and soluble target proteins. Expand
Role of protein-glutathione contacts in defining glutaredoxin-3 [2Fe–2S] cluster chirality, ligand exchange and transfer chemistry
TLDR
Kinetic analysis of cluster transfer from holo derivatives to apo Fdx1 has led to a mechanistic model for cluster transfer chemistry of native holo Grx3, and identification of the likely rate-limiting step for the reaction. Expand
Glutathione-complexed [2Fe-2S] clusters function in Fe–S cluster storage and trafficking
TLDR
The results indicate that the [2Fe-2S](GS4) complex is stable under physiological conditions, and demonstrates reversible cluster exchange with a wide range of Fe–S cluster proteins, thereby supporting a possible physiological role for such centers. Expand
The yeast iron regulatory proteins Grx3/4 and Fra2 form heterodimeric complexes containing a [2Fe-2S] cluster with cysteinyl and histidyl ligation.
TLDR
Analytical, spectroscopic, and mutagenesis data indicate that the ability of the Fra2-Grx3/4 complex to assemble a [2Fe-2S] cluster may act as a signal to control the iron regulon in response to cellular iron status in yeast. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 71 REFERENCES
Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor.
  • C. Lillig, C. Berndt, +4 authors A. Holmgren
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 2005
TLDR
It is proposed that the iron-sulfur cluster serves as a redox sensor for the activation of Grx2 during conditions of oxidative stress when free radicals are formed and the glutathione pool becomes oxidized. Expand
CGFS-type monothiol glutaredoxins from the cyanobacterium Synechocystis PCC6803 and other evolutionary distant model organisms possess a glutathione-ligated [2Fe-2S] cluster.
TLDR
The biochemical characterization of several monothiol Grxs from the cyanobacteria Gloeobacter violaceus and Thermosynechococcus elongatus, the yeast Saccharomyces cerevisiae, the plant Arabidopsis thaliana, and human indicate that the incorporation of a GSH-ligated [2Fe-2S] center is a common feature of prokaryotic and eukaryotic CGFS-active site monothiola Grxs. Expand
AtGRXcp, an Arabidopsis Chloroplastic Glutaredoxin, Is Critical for Protection against Protein Oxidative Damage*
TLDR
It is demonstrated that a plant protein, AtGRXcp, is a chloroplast-localized monothiol Grx with high similarity to yeast Grx5 and a conserved biological function in protecting cells against protein oxidative damage. Expand
Grx5 Glutaredoxin Plays a Central Role in Protection against Protein Oxidative Damage inSaccharomyces cerevisiae
TLDR
The synthetic lethality of the grx5 and grx2 mutations on one hand and ofgrx5 with thegrx3 grx4 combination on the other points to a complex functional relationship among yeast glutaredoxins, with Grx5 playing a specially important role in protection against oxidative stress both during ordinary growth conditions and after externally induced damage. Expand
Functional, structural, and spectroscopic characterization of a glutathione-ligated [2Fe–2S] cluster in poplar glutaredoxin C1
TLDR
Analytical and spectroscopic studies of wild-type protein and site-directed variants and structural characterization of the holoprotein indicate that theholoprotein contains a subunit-bridging [2Fe–2S] cluster that is ligated by the catalytic cysteine of two glutaredoxins and the cysteines of three glutathiones. Expand
Evolution and Cellular Function of Monothiol Glutaredoxins: Involvement in Iron-Sulphur Cluster Assembly
TLDR
Sequence comparison techniques and cladistics indicate that the other two monothiol glutaredoxins of S. cerevisiae, Grx3 and Grx4, have evolved from the fusion of a thioredoxin gene with a monothiotoxin gene early in the eukaryotic lineage, leading to differential functional specialization. Expand
Structure-Function Analysis of Yeast Grx5 Monothiol Glutaredoxin Defines Essential Amino Acids for the Function of the Protein*
TLDR
For all changes studied, there was a correlation between the effects on several different phenotypes: sensitivity to oxidants, constitutive protein oxidation, ability for respiratory growth, auxotrophy for a number of amino acids, and iron accumulation. Expand
Structural insight into poplar glutaredoxin C1 with a bridging iron-sulfur cluster at the active site.
TLDR
It is proposed that the bridging [2Fe-2S] cluster is coordinated by the first cysteine at the glutaredoxin active site from each subunit of holo Grx-C1, along with two cysteines from two glutathione molecules. Expand
Nuclear Monothiol Glutaredoxins of Saccharomyces cerevisiae Can Function as Mitochondrial Glutaredoxins*
TLDR
It is concluded that dithiol glutaredoxins are functionally divergent from monothiol ones, but the latter can interchange their biological activities when compartment barriers are surpassed. Expand
Components involved in assembly and dislocation of iron–sulfur clusters on the scaffold protein Isu1p
TLDR
By radiolabelling of yeast cells with 55Fe it is demonstrated that Isu1p binds an oxygen‐resistant non‐chelatable Fe/S cluster providing in vivo evidence for a scaffolding function of Isu 1p during Fe/s cluster assembly. Expand
...
1
2
3
4
5
...