Semliki Forest virus capsid protein associates with the 60S ribosomal subunit in infected cells.
Semlike forest virus capsid protein cosedimented with the large ribosomal subunit at 60S in sucrose gradients after treatment of cytoplasm from infected cells with Triton X-100 and EDTA. In CsCl gradients the capsid protein banded with the subunit at a density of 1.56 to 1.57 g/cm3. Most of the capsid protein could be detached from the 60S structure by treatment with 0.8 M KCl. The ribonucleoprotein of the 26S RNA had a sedimentation value of 53S and a density of 1.50 g/cm3 and could thus be separated from the 60S structure. The data suggest that the capsid protein binds to the large ribosomal subunit, but not to the viral 26S RNA.
D002213:Capsid / Q000032:analysis*; D002499:Centrifugation, Density Gradient; D004492:Edetic Acid / Q000494:pharmacology; D006367:HeLa Cells; D011092:Polyethylene Glycols / Q000494:pharmacology; D011485:Protein Binding; D012367:RNA, Viral / Q000032:analysis; D012270:Ribosomes / Q000032:analysis*; D012672:Semliki forest virus / Q000032:analysis*; D014764:Viral Proteins / Q000032:analysis*
D012367:RNA, Viral; D014764:Viral Proteins; D011092:Polyethylene Glycols; D004492:Edetic Acid