Article
- The EMBO Journal (2008) 27, 1122 - 1133
- doi:10.1038/emboj.2008.50
Published online: 20 March 2008
Subject Categories:
Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe–2S] clusters
Sibali Bandyopadhyay1,6, Filipe Gama2,6, Maria Micaela Molina-Navarro3, José Manuel Gualberto4, Ronald Claxton1, Sunil G Naik5, Boi Hanh Huynh5, Enrique Herrero3, Jean Pierre Jacquot2, Michael K Johnson1 and Nicolas Rouhier2
- Department of Chemistry, Centre for Metalloenzyme Studies, University of Georgia, Athens, GA, USA
- UMR 1136 IaM, IFR 110, Faculté des Sciences, Nancy University, Vandoeuvre, France
- Department of Basic Medical Sciences, University of Lleida, Lleida, Spain
- Institut de Biologie Moléculaire des Plantes, CNRS, Strasbourg, France
- Department of Physics, Emory University, Atlanta, GA, USA
Correspondence to:
Nicolas Rouhier, UMR 1136 IaM, IFR 110, Faculté des Sciences, Nancy University, Vandoeuvre 54506, France. Tel.: +33 3 83684225; Fax: +33 3 83684292; E-mail: nrouhier@scbiol.uhp-nancy.fr
Michael K Johnson, Department of Chemistry, Centre for Metalloenzyme Studies, University of Georgia, Athens, GA, USA. Tel.: +1 706 542 9378; Fax: +1 706 542 9454; E-mail: johnson@chem.uga.edu
6These authors contributed equally to this work
Received 27 September 2007; Accepted 25 February 2008
Abstract
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] cluster in apo-GrxS14. These Grxs possess the same monothiol CGFS active site as yeast Grx5 and both were able to complement a yeast grx5 mutant defective in Fe–S cluster assembly. In vitro kinetic studies monitored by CD spectroscopy indicate that [2Fe–2S] clusters on GrxS14 are rapidly and quantitatively transferred to apo chloroplast ferredoxin. These data demonstrate that chloroplast CGFS Grxs have the potential to function as scaffold proteins for the assembly of [2Fe–2S] clusters that can be transferred intact to physiologically relevant acceptor proteins. Alternatively, they may function in the storage and/or delivery of preformed Fe–S clusters or in the regulation of the chloroplastic Fe–S cluster assembly machinery.
Keywords:
- chloroplast,
- glutaredoxin,
- iron–sulphur protein,
- plant
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