Reconstitution of functionally active ribosomes from inactive subparticles and proteins.

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Abstract
TheFe are several previous reports which suggest that the physical reconstitution of ribosomes from subcomponents in vitro has been accomplished. However, no demonstration of the reconstitution of functionally active ribosomes has been made. The present results demonstrate the reconstitution of functionally active 50S and 30S ribosomes from inactive subparticles and a mixture of proteins, which comprise about 40% of the total ribosomal proteins. Using essentially the same system, Staehelin and Meselson have also demonstrated the reconstitution of functionally active ribosomes. Since the components necessary for the reconstitution, subparticles and split-proteins, were obtained from purified ribosomes, and the reconstitution can take place in the cold without any other factor, it is concluded that the information for the correct assembly must be contained in the structure of the subcomponents. No external template or enzyme appears to be necessary. Thus, the present results support the hypothesis that at least part of the assembly of the ribosome is an orderly, self-assembly process, which is not directed by other pre-existing cell structures.

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