Abstract
Human ribonucleotide reductase (RR) small subunits, M2 and P53R2, play key roles in forming RR holoenzyme and supplying nucleotide precursors for DNA replication and repair. Currently, we are studying the redox property, structure, and function of hRRM2 and p53R2. In the cell-free system, p53R2 did not oxidize a reactive oxygen species (ROS) indicator Carboxy-H(2)DCFDA, but hRRM2 did. Further studies demonstrated that purified recombinant p53R2 protein has the catalase activity to scavenge H(2)O(2). Over-expression of p53R2 reduced intracellular ROS and protected the mitochondrial membrane potential against oxidative stress, whereas over-expression of hRRM2 did not result in the collapse of mitochondrial membrane potential. Our findings suggest that p53R2 may play a key role in defending oxidative stress by scavenging ROS, and this antioxidant property is also important for its enzymatic activity.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Cell Cycle Proteins / isolation & purification
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Cell Cycle Proteins / metabolism*
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Fluoresceins / metabolism
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Free Radical Scavengers / metabolism
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Genetic Vectors / genetics
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Humans
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Hydrogen Peroxide / pharmacology
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Membrane Potential, Mitochondrial / drug effects
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Mitochondrial Membranes / drug effects
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Mitochondrial Membranes / enzymology
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Oxidation-Reduction / drug effects
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Protein Subunits / metabolism*
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Recombinant Proteins / metabolism
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Ribonucleoside Diphosphate Reductase / isolation & purification
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Ribonucleoside Diphosphate Reductase / metabolism*
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Ribonucleotide Reductases / isolation & purification
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Ribonucleotide Reductases / metabolism*
Substances
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Cell Cycle Proteins
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Fluoresceins
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Free Radical Scavengers
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Protein Subunits
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Recombinant Proteins
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diacetyldichlorofluorescein
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Hydrogen Peroxide
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RRM2B protein, human
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Ribonucleotide Reductases
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ribonucleotide reductase M2
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Ribonucleoside Diphosphate Reductase