A cellular protein phosphorylated by the avian sarcoma virus transforming gene product is associated with ribonucleoprotein particles.
AUTOR(ES)
Arrigo, A P
RESUMO
In chick embryo fibroblasts transformed by Rous sarcoma virus (RSV) the tyrosine phosphorylation of a cellular protein of 34,000 daltons mol. wt. (34 kd) is greatly enhanced; this was shown to be catalyzed by the phosphotransferase activity of RSV transforming protein pp60src. We report here that in cytoplasmic extracts of both normal and transformed cells, in the presence of magnesium ions, the majority of the 34-kd protein is associated with large structures and that a fraction of 34 kd appears to be associated with ribonucleoprotein particles (RNPs). In addition, upon u.v. light cross-linking of RNA to protein in normal or transformed cells, an anti-34 kd serum immunoprecipitates RNA fragments of apparent low sequence complexity as detected by T1 fingerprint analysis. Our results indicate that the 34-kd protein may play a role in the cell at the level of RNPs.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=555134Documentos Relacionados
- Evidence that the avian sarcoma virus transforming gene product is a cyclic AMP-independent protein kinase.
- Protein kinase activity associated with the avian sarcoma virus src gene product.
- The same normal cell protein is phosphorylated after transformation by avian sarcoma viruses with unrelated transforming genes.
- Avian sarcoma virus UR2 encodes a transforming protein which is associated with a unique protein kinase activity.
- Uninfected vertebrate cells contain a protein that is closely related to the product of the avian sarcoma virus transforming gene (src).