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Originally published In Press as doi:10.1074/jbc.M103743200 on June 26, 2001

J. Biol. Chem., Vol. 276, Issue 36, 33488-33494, September 7, 2001
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The Anaerobic Ribonucleotide Reductase from Lactococcus lactis
INTERACTIONS BETWEEN THE TWO PROTEINS NrdD AND NrdG*

Eduard TorrentsDagger §, Rolf EliassonDagger , Henriette Wolpher||, Astrid Gräslund||, and Peter ReichardDagger **

From the Dagger  Department of Biochemistry, Medical Nobel Institute, MBB, Karolinska Institutet, SE-17177 Stockholm Sweden, § Bacterial Molecular Genetics Institut de Biotecnologia i Biomedicina, Universitat Autònoma de Barcelona, E-08193 Bellaterra, Barcelona, and the || Department of Biochemistry and Biophysics, Stockholm University, SE-10691 Stockholm Sweden

Deoxyribonucleotide synthesis by anaerobic class III ribonucleotide reductases requires two proteins, NrdD and NrdG. NrdD contains catalytic and allosteric sites and, in its active form, a stable glycyl radical. This radical is generated by NrdG with its [4Fe-4S]+ cluster and S-adenosylmethionine. We now find that NrdD and NrdG from Lactobacillus lactis anaerobically form a tight alpha 2beta 2 complex, suggesting that radical generation by NrdG and radical transfer to the specific glycine residue of NrdD occurs within the complex. Activated NrdD was separated from NrdG by anaerobic affinity chromatography on dATP-Sepharose without loss of its glycyl radical. NrdD alone then catalyzed the reduction of CTP with formate as the electron donor and ATP as the allosteric effector. The reaction required Mg2+ and was stimulated by K+ but not by dithiothreitol. Thus NrdD is the actual reductase, and NrdG is an activase, making class III reductases highly similar to pyruvate formate lyase and its activase and suggesting a common root for the two anaerobic enzymes during early evolution. Our results further support the contention that ribonucleotide reduction during transition from an RNA world to a DNA world started with a class III-like enzyme from which other reductases evolved when oxygen appeared on earth.

* This work was supported in part by grants from the Karolinska Institutet and the Wallenberg Foundation (to P. R.) and by grants from the Swedish Natural Science Research Council, the Swedish Foundation for Strategic Research (Nucleic Acids Research program), and by European Union Training and Mobility of Researchers network Grant ERBFMRXCT98027 (to A. G.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported in part by a grant from Margit and Folke Pehrzon Foundation.

** To whom correspondence should be addressed: Dept. of Biochemistry 1, Karolinska Institute, S.E.-17177 Stockholm, Sweden. E-mail: peter.reichard@mbb.ki.se.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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