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p53 domains: structure, oligomerization, and transformation

P Wang1, M Reed, Y Wang

  • 1Department of Molecular Genetics and Microbiology, State University of New York, Stony Brook 11794.

Molecular and Cellular Biology
|August 1, 1994
PubMed
Summary
This summary is machine-generated.

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Wild-type p53 protein has distinct structural domains. A globular DNA-binding region and a C-terminal tetramerization domain explain its complex oligomerization and oncogenic potential.

Area of Science:

  • Molecular Biology
  • Protein Structure and Function

Background:

  • Wild-type p53 protein exhibits complex oligomerization behavior, forming tetramers and higher-order structures.
  • Previous studies suggest p53's non-globular shape based on differing gel filtration and sedimentation analyses.

Purpose of the Study:

  • To identify and characterize the structural and oligomerization domains within the p53 protein.
  • To investigate the physical properties of purified p53 segments and their oligomeric behavior.

Main Methods:

  • Analysis of purified p53 segments using sedimentation, gel filtration, and gel electrophoresis.
  • Investigating the oligomerization properties of specific p53 domains, including the DNA-binding region and C-terminus.

Main Results:

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  • The central DNA-binding domain (aa 80-320 murine, aa 83-323 human) is predominantly globular and forms transient oligomers.
  • The C-terminal region (aa 280-390 murine, aa 283-393 human) exhibits non-globular behavior, with a specific segment (aa 315-350 murine, aa 323-355 human) sufficient for stable tetramer formation.
  • The tetramerization domain is crucial for oncogenic transformation, while the DNA-binding domain's oligomerization role in transformation is less clear.

Conclusions:

  • p53 possesses at least two autonomous oligomerization domains: a strong C-terminal tetramerization domain and a weaker central DNA-binding domain.
  • These domains collectively explain the formation of tetramers and higher-order structures by wild-type p53.
  • The C-terminal tetramerization domain is a key determinant of the dominant-negative phenotype in mutant p53-mediated transformation.