Characterization of functional domains of p21 ras by use of chimeric genes

EMBO J. 1985 Feb;4(2):407-12. doi: 10.1002/j.1460-2075.1985.tb03643.x.

Abstract

Comparison of the predicted amino acid sequences of different members of the ras family in vertebrates has shown that the N-terminal 120 residues are highly conserved while the C terminus is variable. To test the possible role of the variable residues in cell transformation, chimeras were constructed containing the N-terminal 111 amino acids of the human Ha-ras EJ oncogene and the C terminus of two Drosophila ras genes. We show that one of these constructs which has only 20 conserved residues between positions 121 and 189, can transform rat-1 cells, and the transformed cells are capable of inducing lethal tumors in rats. The second construct containing the C terminus of another Drosophila ras gene exhibits a transforming capacity as well, but only after linkage to a viral transcriptional promoter. These results show that the majority of residues within the C terminus can be replaced without abolishing the transforming potential of p21 ras.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Transformation, Neoplastic*
  • Cells, Cultured
  • DNA / genetics
  • DNA, Recombinant
  • Drosophila melanogaster
  • GTP-Binding Proteins / genetics
  • Humans
  • Neoplasm Proteins / genetics*
  • Neoplasms, Experimental / genetics*
  • Oncogenes*
  • Proto-Oncogene Proteins p21(ras)
  • Rats
  • Structure-Activity Relationship

Substances

  • DNA, Recombinant
  • Neoplasm Proteins
  • DNA
  • GTP-Binding Proteins
  • HRAS protein, human
  • Proto-Oncogene Proteins p21(ras)

Associated data

  • GENBANK/X02200