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PMID:7824276

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Citation

Hainaut, P, Rolley, N, Davies, M and Milner, J (1995) Modulation by copper of p53 conformation and sequence-specific DNA binding: role for Cu(II)/Cu(I) redox mechanism. Oncogene 10:27-32

Abstract

The tumor suppressor protein p53 is a metal-binding transcription factor whose conformation and function are altered by mutation in cancers. Using murine p53 translated in vitro, we report here that concentrations of copper within the physiological range (< 30 microM) alter the conformation of wild-type p53 and inhibit sequence-specific DNA-binding. Direct binding of copper to p53 in the form of Cu(I) was demonstrated by Electron Spin Resonance using a purified recombinant protein containing residues 1-343 of murine wild-type p53 fused to E. coli maltose binding protein. Moreover, protection against the effect of Cu(II) sulfate was achieved by the Cu(I)-specific chelator bathocuproinedisulfonic acid but not by scavengers of reactive oxygen species, suggesting that alteration of p53 by copper depends upon a Cu(II)/Cu(I) redox mechanism, but does not require the production of reactive oxygen species. Thus copper at physiological concentrations can interact with wild-type p53 and affect its DNA-binding capacity.

Links

PubMed

Keywords

Animals; Base Sequence; Copper/metabolism; DNA/metabolism; Electron Spin Resonance Spectroscopy; Mice; Molecular Sequence Data; Oxidation-Reduction; Protein Binding; Protein Conformation; Tumor Suppressor Protein p53/chemistry; Tumor Suppressor Protein p53/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:P53

enables

GO:0005507: copper ion binding

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete


See also

References

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