Solubilization of a protein synthesis inhibitor from vaccinia virions.
The protein synthesis inhibitor previously demonstrated to be associated with vaccinia cores was quantitatively solubilized from vaccinia virions or cores after an endogenous protein kinase reaction at pH 10. The presence of the inhibitor in the soluble extract correlated with the presence of soluble virion proteins phosphorylated in vitro. Partially purified inhibitor blocked methionyl-tRNAfMet-40S initiation complex formation, as was the case in cell-free extracts derived from vaccinia virus-infected cells.
D006863:Hydrogen-Ion Concentration; D010442:Peptide Chain Initiation, Translational; D010766:Phosphorylation; D014176:Protein Biosynthesis; D011494:Protein Kinases / Q000378:metabolism; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism; D012358:RNA, Transfer, Met; D012270:Ribosomes / Q000378:metabolism; D012995:Solubility; D014616:Vaccinia virus / Q000032:analysis*; D014764:Viral Proteins / Q000302:isolation & purification* / Q000378:metabolism / Q000494:pharmacology; D014771:Virion / Q000032:analysis
D012346:RNA, Transfer, Amino Acyl; D012358:RNA, Transfer, Met; D014764:Viral Proteins; C024988:tRNA, formylmethionine-; D011494:Protein Kinases