Sequence-specific interaction of a conformational domain of p53 with DNA. Academic Article

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.

authors

• Maxwell, Steven

published proceedings

• Cancer Res

author list (cited authors)

• Srinivasan, R., Roth, J. A., & Maxwell, S. A.

citation count

• 18

complete list of authors

• Srinivasan, R||Roth, JA||Maxwell, SA

publication date

• November 1993

published in

• Cancer Research  Journal

keywords

• Animals
• Antigens, Polyomavirus Transforming
• Base Sequence
• Cattle
• Conserved Sequence
• DNA
• Molecular Sequence Data
• Mutation
• Simian Virus 40
• Staphylococcal Protein A
• Tumor Suppressor Protein P53

PubMed Central ID

• 8221671

start page

• 5361

end page

• 5364

volume

• 53

issue

• 22