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Chimaeric alleles were constructed to assay the biological functions of an N-terminal deletion and C-terminal mutations which were found in a naturally occurring mutant of feline vMyc, T17. The mutant alleles were assayed for their ability to transform chick embryo fibroblasts in vitro by a number of criteria, namely the ability to induce morphological transformation, an accelerated growth rate and growth in soft agar. Feline cMyc could transform the avian cells, whilst T17 vMyc could not, and the N-terminal deletion was responsible for conferring the primary transformation defect on the mutant protein. The C-terminal mutations which consist of a point mutation adjacent to the nuclear localisation signal and a point mutation/amino acid insertion within the basic region (BR) could, however, dissociate the Myc-induced parameters of transformation. This effect was a specific function of the BR mutation alone, and the mutation could be transferred into avian cMyc with comparable biological consequences. The BR mutation did not disrupt the sequence specific DNA binding activity of the protein in vivo, despite exerting a biological effect. These data suggest a novel phenotype where the mutation may affect a subset of Myc-regulated genes through altered DNA binding specificity or protein-protein interactions.

Original publication

DOI

10.1093/nar/24.16.3216

Type

Journal article

Journal

Nucleic Acids Res

Publication Date

15/08/1996

Volume

24

Pages

3216 - 3221

Keywords

Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Cats, Cell Transformation, Neoplastic, Chick Embryo, DNA-Binding Proteins, Genes, myc, Molecular Sequence Data, Mutation, Oncogene Protein p55(v-myc), Phenotype, Protein Binding, Protein Structure, Secondary, Proto-Oncogene Proteins c-myc, Recombinant Fusion Proteins, Sequence Deletion