Cloning and characterization of a cDNA from Xenopus laevis coding for a protein homologous to human and murine p53

Oncogene. 1987 Mar;1(1):71-8.


A Xenopus laevis oocyte cDNA library was screened with a murine p53 cDNA probe for the presence of p53-related clones. Several such clones were isolated and analysed. The nucleotide sequence of the largest cDNA clone (2.2 kb) showed a high degree of homology with the human (68%) and murine (70%) p53 coding sequences. This clone contains a single large open-reading frame, coding for a protein of 363 amino acids, which is 51% homologous to human p53 and 57% homologous to murine p53. Furthermore, five highly conserved internal regions were found in all three proteins. The three proteins have a highly similar amino acid composition (including, notably, the presence of a high proportion of proline residues), and they display a comparable distribution of charged amino acids and hydropathic index profile. The in vitro transcription-translation products of the X. laevis clone were successfully immunoprecipitated by human anti-p53 sera, demonstrating that there is at least one epitope in common between the X. laevis protein and human, and possibly murine, p53.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • DNA / genetics
  • DNA Restriction Enzymes
  • Humans
  • Mice
  • Molecular Sequence Data
  • Neoplasm Proteins / genetics*
  • Phosphoproteins / genetics*
  • Protein Conformation
  • RNA, Messenger / genetics
  • Sequence Homology, Nucleic Acid
  • Tumor Suppressor Protein p53
  • Xenopus laevis / genetics*


  • Neoplasm Proteins
  • Phosphoproteins
  • RNA, Messenger
  • Tumor Suppressor Protein p53
  • DNA
  • DNA Restriction Enzymes