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Volume 271, Number 43, Issue of October 25, 1996 pp. 26582-26587
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Allosteric Regulation of the Third Ribonucleotide Reductase (NrdEF Enzyme) from Enterobacteriaceae

(Received for publication, June 28, 1996)

Rolf Eliasson Dagger , Elisabet Pontis Dagger , Albert Jordan Dagger § and Peter Reichard Dagger

From the Dagger  Department of Biochemistry 1, Medical Nobel Institute, MBB, Karolinska Institute, 17177 Stockholm, Sweden and the § Department of Genetics and Microbiology, Faculty of Sciences, Autonomous University of Barcelona, Bellaterra, 08193 Barcelona, Spain

Enterobacteriaceae contain genes for three separate ribonucleotide reductases: nrdAB code for a class Ia enzyme, active during aerobiosis, nrdDG for a class III enzyme, active during anaerobiosis, and nrdEF for a cryptic class Ib enzyme. The NrdEF enzyme provides the active reductase in other, widely different bacteria. Here, we describe the allosteric regulation of the Salmonella typhimurium NrdEF enzyme. It consists of two tightly bound homodimeric proteins, R1E and R2F. Nucleoside triphosphates (ATP, dATP, dGTP, and dTTP) regulate the substrate specificity by binding to a single site of the R1E protein (one nucleotide per polypeptide). Regulation is similar to that of the NrdAB enzyme, with one major exception: dATP stimulates reduction of CDP (and UDP) under conditions when dATP strongly inhibits all activity of the NrdAB enzyme. The nrdA-coded R1 protein contains a second binding site for dATP (and ATP) that controls general enzyme activity. All known R1E proteins lack the 50 N-terminal amino acids of R1, and we propose that the activity site is located in this area of the protein. The more sophisticated regulation of NrdAB enzymes of eukaryotes provides protection against the possibly harmful overproduction of dNTPs.


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