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J. Biol. Chem., Vol. 276, Issue 44, 40647-40651, November 2, 2001
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From the Recently, a homologue of the small subunit of
mammalian ribonucleotide reductase (RNR) was discovered, called p53R2.
Unlike the well characterized S phase-specific RNR R2 protein, the new form was induced in response to DNA damage by the p53 protein. Because
the R2 protein is specifically degraded in late mitosis and absent in
Go/G1 cells, the induction of the p53R2
protein may explain how resting cells can obtain deoxyribonucleotides for DNA repair. However, no direct demonstration of RNR activity of the
p53R2 protein was presented and furthermore, no corresponding RNR large
subunit was identified. In this study we show that recombinant, highly
purified human and mouse p53R2 proteins contain an iron-tyrosyl free
radical center, and both proteins form an active RNR complex with the
human and mouse R1 proteins. UV irradiation of serum-starved, Go/G1-enriched mouse fibroblasts, stably
transformed with an R1 promoter-luciferase reporter gene construct,
caused a 3-fold increase in luciferase activity 24 h after
irradiation, paralleled by an increase in the levels of R1 protein.
Taken together, our data indicate that the R1 protein can
function as the normal partner of the p53R2 protein and that an
R1-p53R2 complex can supply resting cells with deoxyribonucleotides for
DNA repair.
Department of Medical Biochemistry and
Biophysics, Umeå University, SE-901 87 Umeå, Sweden, the
¶ Department of Biophysics, Stockholm University, SE-106 91, Stockholm, Sweden, and the Laboratory of Molecular Medicine,
Human Genome Center, Institute of Medical Science, The University of
Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan
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