p59v-rel, the transforming protein of reticuloendotheliosis virus, is complexed with at least four other proteins in transformed chicken lymphoid cells

• Published in: Journal of Virology Vol. 62; no. 12; pp. 4730 - 4736
• Main Authors: Simek, S, Rice, N.R
• Format: Journal Article
• Language: English
• Published: Washington, DC American Society for Microbiology 01.12.1988
• Subjects: ACTIVIDAD ENZIMATICA; ACTIVITE ENZYMATIQUE; Animals; Biological and medical sciences; Cell Line, Transformed; Centrifugation, Density Gradient; Chickens; Electrophoresis, Polyacrylamide Gel; Fundamental and applied biological sciences. Psychology; Immune Sera; Lymphoid Tissue - cytology; Microbiology; Morphology, structure, chemical composition, physicochemical properties; Oncogene Proteins v-rel; ONCOVIRUS AVIAIRE; ONCOVIRUS AVIAR; POLLO; POULET; Precipitin Tests; Protein Kinases - metabolism; PROTEINAS; PROTEINE; Proteins - metabolism; Proto-Oncogene Proteins - metabolism; Proto-Oncogene Proteins c-rel; Reticuloendotheliosis virus; Retroviridae; Retroviridae Proteins - metabolism; TRANSFERASAS; TRANSFERASE; Virology; Virus; Proteins; Oncovirinae; Lymphoid cell; Immunoprecipitation reaction; Protein kinase; Type C oncovirus; Transformed cell; Avian reticuloendotheliosis virus; Retroviridae; V-Onc gene; Molecular interaction
• ISSN: 0022-538X; 1098-5514
• DOI: 10.1128/jvi.62.12.4730-4736.1988

Previous studies have identified the protein product of v-rel, the oncogene carried by reticuloendotheliosis virus (REV), as a 59,000-dalton phosphoprotein located predominantly in the cytosol of transformed chicken lymphoid cells. In immune precipitates of p59v-rel, there is a closely associated protein kinase activity. In chicken lymphoid cells that do not contain REV, p68c-rel is found free in the cytosol not associated with other proteins and not detectably phosphorylated. In this study, we found that immuneprecipitates of 59v-rel from REV-transformed cells contain at least four other proteins, of approximate molecular weights 124, 115, 68, and 36 kilodaltons (kDa). The 124-, 115-, and 36-kDa proteins are apparently unrelated to p59v-relin sequence, and their coprecipitation suggests that they are complexed with p59v-rel. The coprecipitating 68-kDa protein was found to be p68c-rel which, like the other three proteins, precipitates by virtue of its association with p59v-rel. Glycerol gradient analysis suggested the presence of more than onetype of complex: one containing p115, p68c-rel, p59v-rel, and p36, and another containing p124, p115, p59v-rel and possibly p68c-rel. In vitro kinase activitywas found in all size classes, coinciding with the distribution of p115 and p59v-rel. The complex(es) was stable under a variety of conditions, including awide range of ionic strengths, chelators, and detergents, and through multiple cycles of immune precipitation and elution. This suggests a specific and functionally significant interaction among the members that may be of direct relevance to the mechanism of REV-induced transformation