The genome of reticuloendotheliosis virus T (REV-T) includes a unique oncogene v-rel, which is transcribed in low amounts into a 3.0-kilobase
subgenomic mRNA in REV-T-transformed lymphoid cells. To identify the
v-rel protein, REV-
T DNA sequences were cloned into bacterial plasmid vectors designed to achieve expression of foreign DNA sequences in Escherichia coli. Portions of the v-rel gene were joined to the 5' segment of the trpE gene. Upon induction of trpE with
indoleacrylic acid, large amounts of trpE-v-rel fusion
proteins were produced by the bacteria carrying these recombinant plasmids. Two trpE-v-rel fusion
proteins were synthesized in E. coli, which collectively represent three-quarters of the predicted
v-rel protein. Polyclonal
antisera were generated to trpE-v-red fusion
proteins. These
antisera were used in immunoblotting experiments to identify a 57-kDa
v-rel protein in REV-T-transformed lymphoid cells lines and REV-T-infected chicken embryo fibroblast cultures. The v-rel gene expressed in E. coli under lac control was found to produce a 56-kDa
protein. Although REV-T-transformed and
Marek disease virus-transformed lymphoid cells contain c-rel
mRNA transcripts, a
c-rel protein could not be detected with
antisera directed against v-rel fusion
proteins.