Abstract
The messenger function of Sendai virus ribonucleoprotein (RNP) was examined in a cell-free system using ribosomes from Ehrlich tumor and chick embryo cells. RNP obtained by treatment of virions with 0.5% sodium deoxycholate, preincubated with ribonuclease, and purified by banding in CsCl density gradient (ϱ = 1.31 g/cm 3), was able to associate with ribosomes, forming complexes that sedimented at 160 S, 180 S, and, predominantly, at > 300 S when centrifuged in sucrose gradients. The buoyant density of the complexes in CsCl was 1.43 g/cm 3 while the complexes formed between viral RNA and ribosomes had a buoyant density of 1.57 g/cm 3. Dissociation of the complexes with EDTA and RNase released the RNP with buoyant density of 1.35 and 1.31 g/cm 3, respectively. The complexes incorporated labeled amino acids, the incorporation being inhibited by puromycin. The plateau in amino acid incorporation was reached when 40 μg of RNA in RNP per 500 μg of ribosomes was used.
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