Abstract
Publisher Summary This chapter describes that the bacterial ribosome is a noncovalent complex made up of three molecules of RNA, over fifty different protein molecules, and certain monovalent and bivalent cations, arranged in two interacting but separable subunits. The ribosome is the site of protein synthesis and carries at least two catalytic sites that participate in this process, and serves as the focus and organizing center of the protein-synthesizing apparatus. As such, it interacts with other macromolecular components of the apparatus: messenger RNA, aminoacyl- and peptidyl-tRNAs, and the numerous protein factors that assist in peptide chain initiation, elongation and termination. Each of these ligands interacts with a specific binding site on the surface of the ribosome in a strictly controlled sequence: binding; acting on or being acted on by the ribosome; in some cases, being transferred to a different site; and eventually becoming detached. The chapter discusses the experiments having to do with the nature of the ribosomal proteins, protein-RNA interactions, conformation and conformational changes, and the specific cations required for the structural integrity of the ribosome.
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