title: The Synechocystis PCC6803 MerA-like enzyme operates in the reduction of both mercury and uranium under the control of the glutaredoxin 1 enzyme.
abstract: In a continuing effort to analyze the selectivity/redundancy of the three glutaredoxin (Grx) enzymes of the model cyanobacterium Synechocystis PCC6803, we have characterized an enzyme system that plays a crucial role in protection against two toxic metal pollutants, mercury and uranium. The present data show that Grx1 (Slr1562 in CyanoBase) selectively interacts with the presumptive mercuric reductase protein (Slr1849). This MerA enzyme plays a crucial role in cell defense against both mercuric and uranyl ions, in catalyzing their NADPH-driven reduction. Like MerA, Grx1 operates in cell protection against both mercury and uranium. The Grx1-MerA interaction requires cysteine 86 (C86) of Grx1 and C78 of MerA, which is critical for its reductase activity. MerA can be inhibited by glutathionylation and subsequently reactivated by Grx1, likely through deglutathionylation. The two Grx1 residues C31, which belongs to the redox active site (CX(2)C), and C86, which operates in MerA interactions, are both required for reactivation of MerA. These novel findings emphasize the role of glutaredoxins in tolerance to metal stress as well as the evolutionary conservation of the glutathionylation process, so far described mostly for eukaryotes.
authors.affiliation: UMR8221, CEA, CNRS, Université Paris Sud, iBiTec-S, LBBC, Gif sur Yvette, France.
authors.forename: Benoit
authors.initials: B
authors.lastname: Marteyn
authors.forename: Samer
authors.initials: S
authors.lastname: Sakr
authors.forename: Sandrine
authors.initials: S
authors.lastname: Farci
authors.forename: Mariette
authors.initials: M
authors.lastname: Bedhomme
authors.forename: Solenne
authors.initials: S
authors.lastname: Chardonnet
authors.forename: Paulette
authors.initials: P
authors.lastname: Decottignies
authors.forename: Stéphane D
authors.initials: SD
authors.lastname: Lemaire
authors.forename: Corinne
authors.initials: C
authors.lastname: Cassier-Chauvat
authors.forename: Franck
authors.initials: F
authors.lastname: Chauvat
mesh_terms: D015964:Gene Expression Regulation, Bacterial; D015971:Gene Expression Regulation, Enzymologic; D054477:Glutaredoxins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008628:Mercury / Q000378:metabolism* / Q000633:toxicity; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D054730:Protein Interaction Domains and Motifs; D046939:Synechocystis / Q000187:drug effects* / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D020798:Two-Hybrid System Techniques; D014501:Uranium / Q000378:metabolism / Q000633:toxicity
chemical_list: D054477:Glutaredoxins; D014501:Uranium; D010088:Oxidoreductases; C021551:mercuric reductase; D008628:Mercury