Abstract
The elucidation of how RNA and proteins axe assembled in the ribosomal particles of Escherichia coli is important for an understanding of their involvement in the translation of the genetic code. Chain initiation and termination are very likely targets of specific regulatory signals operating at the translation level. The elucidation of the detailed molecular events occurring at these steps will be important for understanding translational control of protein synthesis. With respect to chain termination, the evidence on the aggregation of protein subunits (identical or nonidentical) at the ribosomal level and its possible role in the release of finished chains, indicates the importance in chain termination of signals other than code signals. The possible function of subunit aggregation as a control mechanism in protein synthesis emphasized that the attachment of nonpeptide groups to growing or finished chains could regulate the activation of a chain-release mechanism, possibly through conformational changes of the polypeptide chain. The spatial organization of the polysomes within the cell, (the significance and mode of association of polysomes with membranes), the possible topographical segregation (structural or functional) of individual polysomes (or groups of functionally related polysomes) and their ancillary free ribosomes and the influence that these topographical factors have on the functioning of the protein-synthesis should be investigated.