Abstract
Reticulocyte ribosomes were dissociated under various conditions and the release of 5S RNA was assayed. The 5S RNA was released from ribosomes suspended in Tris buffer, pH 9.5, containing EDTA or in Tris buffer, pH 9.5, after dialysis against the same buffer. Only negligible amounts of protein were solubilized during the removal of the 5S RNA. The particles devoid of 5S RNA had a slightly lower sedimentation coefficient than particles retaining 5S RNA formed through treatment of ribosomes with Tris buffer, pH 9.5, or Tris buffer, pH 7.4, with EDTA or high salt concentrations. The 5S RNA-free particles, when dialyzed against high Mg Tris buffer, pH 7.4, refolded to a more compact form with a sedimentation coefficient close to the 60S subunit. During refolding of the latter particle there was no specific reattachment of 5S RNA.
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