Unknown

Dataset Information

0

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.

PROVIDER: S-EPMC4148882 | BioStudies |

REPOSITORIES: biostudies

Similar Datasets

| S-EPMC5258196 | BioStudies
| S-EPMC3331715 | BioStudies
| S-EPMC3013046 | BioStudies
| S-EPMC7170024 | BioStudies
| S-EPMC3236052 | BioStudies
2009-01-01 | S-EPMC2796373 | BioStudies
| S-EPMC3448021 | BioStudies
| S-EPMC5077177 | BioStudies
| S-EPMC3964038 | BioStudies
| S-EPMC7837452 | BioStudies