title: Structural and spectroscopic insights into BolA-glutaredoxin complexes.
abstract: BolA proteins are defined as stress-responsive transcriptional regulators, but they also participate in iron metabolism. Although they can form [2Fe-2S]-containing complexes with monothiol glutaredoxins (Grx), structural details are lacking. Three Arabidopsis thaliana BolA structures were solved. They differ primarily by the size of a loop referred to as the variable [H/C] loop, which contains an important cysteine (BolA_C group) or histidine (BolA_H group) residue. From three-dimensional modeling and spectroscopic analyses of A. thaliana GrxS14-BolA1 holo-heterodimer (BolA_H), we provide evidence for the coordination of a Rieske-type [2Fe-2S] cluster. For BolA_C members, the cysteine could replace the histidine as a ligand. NMR interaction experiments using apoproteins indicate that a completely different heterodimer was formed involving the nucleic acid binding site of BolA and the C-terminal tail of Grx. The possible biological importance of these complexes is discussed considering the physiological functions previously assigned to BolA and to Grx-BolA or Grx-Grx complexes.
authors.affiliation: From the Université de Lorraine and CNRS, UMR 7036 CRM2, BioMod group, 54506 Vandœuvre-lès-Nancy, France.
authors.forename: Thomas
authors.initials: T
authors.lastname: Roret
authors.affiliation: From the Université de Lorraine and CNRS, UMR 7036 CRM2, BioMod group, 54506 Vandœuvre-lès-Nancy, France.
authors.forename: Pascale
authors.initials: P
authors.lastname: Tsan
authors.affiliation: Université de Lorraine, UMR 1136 Interactions Arbres Microorganismes, F-54500 Vandœuvre-lès-Nancy, France, INRA, UMR 1136 Interactions Arbres Microorganismes, F-54280 Champenoux, France, and.
authors.forename: Jérémy
authors.initials: J
authors.lastname: Couturier
authors.affiliation: Department of Chemistry and Center for Metalloenzyme Studies, University of Georgia, Athens, Georgia 30602.
authors.forename: Bo
authors.initials: B
authors.lastname: Zhang
authors.affiliation: Department of Chemistry and Center for Metalloenzyme Studies, University of Georgia, Athens, Georgia 30602.
authors.forename: Michael K
authors.initials: MK
authors.lastname: Johnson
authors.affiliation: Université de Lorraine, UMR 1136 Interactions Arbres Microorganismes, F-54500 Vandœuvre-lès-Nancy, France, INRA, UMR 1136 Interactions Arbres Microorganismes, F-54280 Champenoux, France, and.
authors.forename: Nicolas
authors.initials: N
authors.lastname: Rouhier
authors.affiliation: From the Université de Lorraine and CNRS, UMR 7036 CRM2, BioMod group, 54506 Vandœuvre-lès-Nancy, France, claude.didierjean@univ-lorraine.fr.
authors.forename: Claude
authors.initials: C
authors.lastname: Didierjean
mesh_terms: D017360:Arabidopsis / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000737:chemistry*; D001483:Base Sequence; D017931:DNA Primers; D004268:DNA-Binding Proteins / Q000737:chemistry*; D054477:Glutaredoxins / Q000737:chemistry*; D007501:Iron / Q000378:metabolism; D008958:Models, Molecular; D013057:Spectrum Analysis / Q000379:methods
chemical_list: D029681:Arabidopsis Proteins; C000589128:BolA protein, Arabidopsis; D017931:DNA Primers; D004268:DNA-Binding Proteins; D054477:Glutaredoxins; D007501:Iron
keywords: BolA; Complexes; Glutaredoxin; Glutathione; Iron Metabolism; Iron-Sulfur Protein; Redox Regulation; Thiol