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Science 18 June 1993:
Vol. 260. no. 5115, pp. 1773 - 1777
DOI: 10.1126/science.8511586
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Articles

Science, Vol 260, Issue 5115, 1773-1777
Copyright © 1993 by American Association for the Advancement of Science

articles

From RNA to DNA, why so many ribonucleotide reductases?

P Reichard

Department of Biochemistry I, Karolinska Institute, Stockholm, Sweden.

It is generally accepted that DNA appeared after RNA during the chemical evolution of life. To synthesize DNA, deoxyribonucleotides are required as building blocks. At present, these are formed from the corresponding ribonucleotides through the enzymatic action of ribonucleotide reductases. Three classes of enzymes are present in various organisms. There is little sequence similarity among the three classes of reductases. However, enzymic mechanisms and the allosteric behavior of the enzymes from various organisms are strongly conserved, suggesting that the enzymes might have evolved from a common ancestor, with the class III anaerobic Escherichia coli reductase as its closest relative.


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Mammalian p53R2 Protein Forms an Active Ribonucleotide Reductase in Vitro with the R1 Protein, Which Is Expressed Both in Resting Cells in Response to DNA Damage and in Proliferating Cells.
O. Guittet, P. Hakansson, N. Voevodskaya, S. Fridd, A. Graslund, H. Arakawa, Y. Nakamura, and L. Thelander (2001)
J. Biol. Chem. 276, 40647-40651
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Structure-Function Investigation of the Interaction of 1- and 2-Substituted 3-Hydroxypyridin-4-ones with 5-Lipoxygenase and Ribonucleotide Reductase.
R. Kayyali, J. B. Porter, Z. D. Liu, N. A. Davies, J. H. Nugent, C. E. Cooper, and R. C. Hider (2001)
J. Biol. Chem. 276, 48814-48822
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Science. ISSN 0036-8075 (print), 1095-9203 (online)