Viral rel and cellular rel associate with cellular proteins in transformed and normal cells.

The rel oncogene from the avian reticuloendotheliosis virus strain T is a 59 kd phosphoprotein localized primarily to the cytoplasm of transformed cells. Recently, the v-rel protein was shown to associate with several cellular proteins with molecular weights of 124 kd, 115 kd, and 36 kd. We have analysed the subcellular distribution of v-rel protein complexes after biochemical fractionation of [35S]methionine and [32P]orthophosphate labeled cells. Our results demonstrate that the v-rel protein coprecipitates with a characteristic set of proteins, some of which are distinct to nuclear or cytoplasmic fractions. We also demonstrate that the normal cellular homolog of the viral rel protein, c-rel, coprecipitates with several cellular proteins from normal chick hematopoietic tissue. These cellular proteins have apparent molecular weights similar to those which are coprecipitated with v-rel from cytoplasmic fractions. Our results demonstrate that both v-rel and c-rel interact with a variety of cellular proteins and suggest that this association is important for the function or regulation of the rel protein.