Serine phosphorylation of the v-rel oncogene product/pp40 complex.
The transforming protein encoded by the v-rel oncogene of reticuloendotheliosis virus has been purified from REV-T transformed lymphoid cells by sequential DEAE-Sepharose and immunoaffinity chromatography. The purified preparation consisted of pp59v-rel and the 40 kDa cellular protein which is complexed with the v-rel oncogene product in transformed cells as well as some minor proteins. Incubation of this purified preparation in the presence of Mg2+ and (gamma-32P)ATP resulted in phosphorylation of both pp59v-rel and the 40 kDa protein. This preparation was also able to phosphorylate casein on serine residues. Immunoprecipitates obtained from extracts of REV-T transformed lymphoid cells labeled with 32P-orthophosphate contained 59 and 40 kDa phosphoproteins. Both pp59v-rel and the 40 kDa protein were phosphorylated on serine residues in transformed cells.
Tung
H Y
HY
Clayton Foundation Biochemical Institute, University of Texas, Austin 78712.
Bargmann
W J
WJ
Bose
H R
HR
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D002461:Cell Line, Transformed; D008970:Molecular Weight; D020572:Oncogene Proteins v-rel; D010766:Phosphorylation; D001356:Reticuloendotheliosis virus / Q000235:genetics; D012191:Retroviridae Proteins / Q000302:isolation & purification / Q000378:metabolism*; D012694:Serine
D020572:Oncogene Proteins v-rel; D012191:Retroviridae Proteins; D012694:Serine; D000255:Adenosine Triphosphate