Ribosomal Aggregates Engaged in Protein Synthesis : Ergosome Breakdown and Messenger Ribonucleic Acid Transport

Nature ◽  
1963 ◽  
Vol 198 (4881) ◽  
pp. 632-638 ◽  
Author(s):  
HANS NOLL ◽  
THEOPHIL STAEHELIN ◽  
F. O. WETTSTEIN
1976 ◽  
Vol 154 (2) ◽  
pp. 379-385 ◽  
Author(s):  
A Yannarell ◽  
D E. Schumm ◽  
T E Webb

Cytoplasmic macromolecules were previously identified which regulate both qualitatively and quantitatively the release of messenger-like RNA from isolated nuclei. These macromolecules are now shown to be denatured at 45-50 degrees C and their synthesis is sensitive to pactamycin or cycloheximide. The putative regulatory proteins are essentially quantitatively precipitated with high specificity from the cytosol by streptomycin at a concentration 10-fold higher than that used to precipitate RNA. The nuclear concentration-dependence of RNA transport from successive samples of nuclei strongly suggests that the regulatory factors are recycled. Quantitative changes in the sequences transported at various dilutions of the cytosol suggest that not all the different classes of the putative regulatory macromolecules are present in an effective concentration at any one dilution.


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