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Literature summary for 1.17.4.2 extracted from

  • Pontarin, G.; Ferraro, P.; Rampazzo, C.; Kollberg, G.; Holme, E.; Reichard, P.; Bianchi, V.
    Deoxyribonucleotide metabolism in cycling and resting human fibroblasts with a missense mutation in p53R2, a subunit of ribonucleotide reductase (2011), J. Biol. Chem., 286, 11132-11140.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.17.4.2

Cloned(Commentary)

Cloned (Comment) Organism
gene encoding p53R2 genotyping, real-time RT-PCR expression analysis Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information isolation of a p53R2 mutant from skin fibroblasts, quiescent p53R2 mutant cells contain more isozyme R2, incorporate more BrdU into cell nuclei, and synthesize more DNA from dTMP than matched controls Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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 isozymes R2 and p53R2
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Source Tissue

Source Tissue Comment Organism Textmining
fibroblast isozymes R2 and p53R2 Homo sapiens
-

Subunits

Subunits Comment Organism
dimer both subunits are required for catalytic activity Homo sapiens

General Information

General Information Comment Organism
additional information cycling fibroblasts from a patient with a lethal mutation in p53R2 contain a normal amount of mtDNA and show normal growth, ribonucleotide reduction, and deoxynucleoside triphosphate (dNTP) pools. However, when made quiescent by prolonged serum starvation the mutant cells strongly down-regulate ribonucleotide reduction, decrease their dCTP and dGTP pools, and virtually abolish the catabolism of dCTP in substrate cycles. mtDNA is not affected Homo sapiens
physiological function the enzyme is involved in ribonucleotide reduction, that provides deoxynucleotides for nuclear and mitochondrial DNA replication and DNA repair Homo sapiens