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Association Factor of Ribosomal Subunits from Bacillus stearothermophilus

By M. García-Patrone, N. S. González and I. D. Algranati

Abstract

The isolation of a new factor, which can cause the in vitro association of 30S and 50S ribosomal subunits at low Mg(++) concentration, is described. The association factor is eluted together with the dissociation protein when ribosomes of Bacillus stearothermophilus are washed with salt solutions of high concentration. The association activity is heat-stable, whereas dissociation factor is inactivated after 10 min at 80°C. This treatment allows the separation of both factors. Several properties rule out the possibility that uncharged, amino-acyl-, or peptidyl-tRNA are responsible for the association process described in this report. Digestion with trypsin shows that the association factor contains at least two components, one of which is a protein

Topics: Biological Sciences: Biochemistry
Year: 1971
DOI identifier: 10.1073/pnas.68.11.2822
OAI identifier: oai:pubmedcentral.nih.gov:389534
Provided by: PubMed Central
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