Core transcription restores in vitro inhibition of protein synthesis induced by vaccinia virus.
When Ehrlich acistes tumor cell lysate is incubated in the presence of vaccinia core, protein synthesis is impaired. However, when the same system is coupled with viral transcription, protein synthesis is restored. The reversal of endogenous protein synthesis is inhibited by actinomycin D, suggesting that de novo RNA synthesis is required for the reversal of total protein synthesis. When the in vitro products of synthesis are analysed by polyacrylamide gel electrophoresis, two newly synthesized peptides which are not present in the noncoupled transcription-translation system are observed. These two peptides have molecular weights of 31 000 and 25 000, similar to viral early proteins.
D000818:Animals; D002286:Carcinoma, Ehrlich Tumor / Q000378:metabolism; D002472:Cell Transformation, Viral; D002474:Cell-Free System; D003609:Dactinomycin / Q000494:pharmacology; D007700:Kinetics; D051379:Mice; D008970:Molecular Weight; D009363:Neoplasm Proteins / Q000235:genetics; D014176:Protein Biosynthesis / Q000187:drug effects; D014158:Transcription, Genetic / Q000187:drug effects; D014616:Vaccinia virus / Q000235:genetics*; D014764:Viral Proteins / Q000235:genetics
D009363:Neoplasm Proteins; D014764:Viral Proteins; D003609:Dactinomycin