A single amino-acid substitution in the DNA-binding domain of the myb oncogene confers a thermolabile phenotype to E26-transformed myeloid cells.
A biologically active provirus of the ts 143 E26 mutant that is temperature-sensitive (ts) for myeloblast transformation was molecularly cloned. The predicted amino-acid sequence of the v-myb-encoded domain of the mutant P135gag-myb-ets protein displayed two single amino-acid changes, one of which was non-conservative when compared to the wild-type E26 v-myb sequence. This mutation, which substitutes a threonine residue (wild-type) for an arginine residue (mutant), is located within the amino-terminal part of v-myb in the DNA-binding domain at a position which is conserved between the c-myb genes of chicken, humans, mice and Drosophila. Introduction of this mutation into the genome of a wild-type E26 virus was sufficient to induce a ts phenotype similar to that obtained with the original ts 143 E26 virus.
Li
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RP
Laboratoire d'Oncologie Moléculaire, Unité 186 INSERM, CNRS U 1160, Institut Pasteur, Lille, France.
Duterque-Coquillaud
M
M
Lagrou
C
C
Debuire
B
B
Graf
T
T
Stehelin
D
D
Leprince
D
D
D001483:Base Sequence; D002471:Cell Transformation, Neoplastic; D003001:Cloning, Molecular; D004268:DNA-Binding Proteins / Q000235:genetics*; D006358:Hot Temperature; D008969:Molecular Sequence Data; D009154:Mutation; D020626:Oncogene Proteins v-myb; D009857:Oncogenes; D010641:Phenotype; D015682:Retroviridae Proteins, Oncogenic / Q000235:genetics*
D004268:DNA-Binding Proteins; D020626:Oncogene Proteins v-myb; D015682:Retroviridae Proteins, Oncogenic; C050379:oncogene proteins v-ets