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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 coil. Changing the C-terminal end of GrxS7.2, a genuine class Ill glutaredoxin, allowed purifying some holoproteins. These properties are discussed considering the documented function of class III glutaredoxins in development. (C) 2010 Elsevier Inc. All rights reserved.
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https://hal.inrae.fr/hal-02662291
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Submitted on : Saturday, May 30, 2020 - 11:51:03 PM
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Jérémy Couturier, Claude Didierjean, Jean-Pierre Jacquot, Nicolas Rouhier. Engineered mutated glutaredoxins mimicking peculiar plant class III glutaredoxins bind iron-sulfur centers and possess reductase activity. Biochemical and Biophysical Research Communications, Elsevier, 2010, 403 (3-4), pp.435 - 441. ⟨10.1016/j.bbrc.2010.11.050⟩. ⟨hal-02662291⟩

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