Proteins encoded by ras oncogenes stimulate or inhibit phosphorylation of specific mitochondrial membrane proteins.
We have examined the effects of a series of purified p21 proteins encoded by ras oncogenes and synthesized in E. coli via recombinant DNA methods, on the phosphorylation of proteins associated with isolated rat liver mitochondria. We find that these proteins markedly enhance the phosphorylation of a 36KD protein and inhibit phosphorylation of a 17KD protein. The phosphorylated residues on the 36KD protein are hydrolyzed by mild acid, suggesting that they involve phosphoamide bonds. These results suggest that p21 proteins may play a role in vivo by altering the phosphorylation of certain proteins.
D000818:Animals; D006153:Guanosine Diphosphate / Q000378:metabolism; D007425:Intracellular Membranes / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism*; D008930:Mitochondria, Liver / Q000378:metabolism*; D008970:Molecular Weight; D009856:Oncogene Proteins, Viral / Q000378:metabolism*; D009857:Oncogenes; D010750:Phosphoproteins / Q000378:metabolism*; D051381:Rats; D011994:Recombinant Proteins / Q000378:metabolism*
D008565:Membrane Proteins; D009856:Oncogene Proteins, Viral; D010750:Phosphoproteins; D011994:Recombinant Proteins; D006153:Guanosine Diphosphate