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C000895200v1
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Papers In Press, published online ahead of print February 2, 2001
J. Biol. Chem, 10.1074/jbc.C000895200
Submitted on December 19, 2000
Revised on February 1, 2001
Accepted on February 1, 2001

Activation of class III ribonucleotide reductase by thioredoxin

Dominique Padovani, Etienne A. Mulliez, and Marc Fontecave

Biologie Moléculaire et Cellulaire, CEA, Grenoble, cedex 9 38054

Corresponding Author: emulliez{at}cea.fr

SUMMARY Anaerobic ribonucleotide reductase provides facultative and obligate anaerobic microorganisms with the deoxyribonucleoside triphosphates used for DNA chain elongation and repair. In E. coli, the dimeric a2 enzyme contains, in its active form, a glycyl radical essential for the reduction of the substrate. The introduction of the glycyl radical results from the reductive cleavage of S-Adenosyl methionine catalysed by the reduced (4Fe-4S) of a small activating protein called b. This activation reaction has long been known to have an absolute requirement for dithiothreitol. Here, we report that thioredoxin along with NADPH and NADPH :thioredoxin oxidoreductase efficiently replaces dithiothreitol and reduces an unsuspected critical disulfide bond probably located on the C-terminus of the a protein. Activation of reduced a protein does not require dithiothreitol or thioredoxin anymore and activation rates are much faster than previously reported. Thus, in E. coli, thioredoxin has very different roles for class I RNR where it is required for the substrate turnover and class III RNR where it acts only for the activation of the enzyme.


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