title: Engineered mutated glutaredoxins mimicking peculiar plant class III glutaredoxins bind iron-sulfur centers and possess reductase activity.
abstract: In order to gather biochemical information about class III glutaredoxins (CCxC/S active sites), the active sites of two poplar class I glutaredoxins, GrxC1 and C4, CGYC and CPYC, respectively, were transformed into CCMC or CCMS. All the recombinant mutated proteins bind [2Fe-2S] centers into holodimers, whereas monomeric apoforms possess glutathione-dependent reductase activity. The functionally important, hydrophobic GALWL C-terminal end, found in most class III glutaredoxins, prevents expression in Escherichia coli. Changing the C-terminal end of GrxS7.2, a genuine class III glutaredoxin, allowed purifying some holoproteins. These properties are discussed considering the documented function of class III glutaredoxins in development.
authors.affiliation: UMR1136 INRA-Nancy Université, Interactions Arbres/Micro-organismes, IFR110, Faculté des Sciences, BP 239, 54506 Vandoeuvre, France.
authors.forename: Jérémy
authors.initials: J
authors.lastname: Couturier
authors.forename: Claude
authors.initials: C
authors.lastname: Didierjean
authors.forename: Jean-Pierre
authors.initials: JP
authors.lastname: Jacquot
authors.forename: Nicolas
authors.initials: N
authors.lastname: Rouhier
mesh_terms: D000595:Amino Acid Sequence; D054477:Glutaredoxins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D007501:Iron / Q000378:metabolism*; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D032107:Populus / Q000201:enzymology*; D011485:Protein Binding; D011487:Protein Conformation; D015202:Protein Engineering; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013455:Sulfur / Q000378:metabolism*
chemical_list: D054477:Glutaredoxins; D011994:Recombinant Proteins; D013455:Sulfur; D007501:Iron; D010088:Oxidoreductases