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SEQUENCE-SPECIFIC INTERACTION OF A CONFORMATIONAL DOMAIN OF P53 WITH DNA | Academic Article individual record
abstract

Mutations within a conserved \"conformational\" domain of the p53 protein have frequently been observed in a wide variety of human cancers. A hybrid protein containing the wild-type conformational domain of p53 fused to protein A bound to calf thymus DNA and a specific p53 DNA-binding motif. Hybrid proteins containing mutations in p53 bound to DNA less efficiently than wild-type hybrid protein. In addition, competition experiments showed that mutated p53 DNA-binding motif failed to interact with p53 hybrid proteins. The DNA-binding activity of wild-type p53 hybrid protein was inhibited by the metal chelator 1,10-phenanthroline. These results demonstrate that DNA-binding activity resides in the conformational domain of p53, providing a structural model for disruption of DNA binding by mutation. Furthermore, metal ions may regulate binding of p53 to DNA by modulating its conformation.

author list (cited authors)
SRINIVASAN, R., ROTH, J. A., & MAXWELL, S. A.
publication date
1993
published in
keywords
  • Staphylococcal Protein A
  • Mutation
  • DNA
  • Molecular Sequence Data
  • Antigens, Polyomavirus Transforming
  • Tumor Suppressor Protein P53
  • Conserved Sequence
  • Cattle
  • Simian Virus 40
  • Animals
  • Base Sequence
citation count

16