The Transfer RNA Binding Site of the 30 S Ribosome and the Site of Tetracycline Inhibition
This extract was created in the absence of an abstract.
Excerpt
Investigations from a number of laboratories (Hardy et al., 1969; Moore et al., 1968; Fogel and Sypherd, 1968; Kaltschmidt et al., 1967) have demonstrated that Escherichia coli ribosomes are composed of a large number (probably 50 to 55) of chemically distinct proteins. The experiments reported earlier in this volume by Nomura et al. have shown that for the 30 S ribosomal subunit each individual protein makes a measurable contribution to the final ability of the particle to function. Thus the ribosome is a highly complex organelle whose function is intricately dependent on the overall set of interactions of its many components. What is not clear from these results is the question of which proteins should be designated as being directly and intimately responsible for specific functions. It is of basic importance to determine which of the 20 proteins in the 30 S particle are involved in the actual binding of...
