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Isolation of a 5S RNA-Protein Complex from Mammalian Ribosomes
Proceedings of the National Academy of Sciences of the United States of America
Vol. 68, No. 8 (Aug., 1971), pp. 1881-1885
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/61305
Page Count: 5
You can always find the topics here!Topics: RNA, Ribosomes, Magnesium, Gels, Liver, Electrophoresis, Centrifugation, Reticulocytes, Molecular weight, HeLa cells
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5S RNA is removed from the large ribosomal subunit of both rat liver and rabbit reticulocyte ribosomes by treatment with EDTA to remove magnesium ions. The RNA is removed not as a naked molecule, but in association with a single ribosomal protein (molecular weight about 35,000) as a ribonucleoprotein, sedimenting at about 7 S. Conditions for the exclusive removal of the 5S RNA-protein complex have been established. Both ribosomal subunits undergo distinct changes in their sedimentation rate, concomitant with the loss of their biological activity, when sedimented into sucrose gradients containing high concentrations of monovalent ions and low concentrations of magnesium. Under these conditions the large subunit loses 5S RNA, the 5S RNA-associated protein, and several more proteins.
Proceedings of the National Academy of Sciences of the United States of America © 1971 National Academy of Sciences