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EF-G interacts with the ribosome, and upon delivery to the ribosome of the ratcheted mRNA, causes the ribosome to adopt an opened configuration. The ratcheting step requires energy and at least a 50-50 mixture of the GTP-bound and GDP-bound forms of EF-G; hence the stoichiometry is favorably set so that when EB-Tu, Phe-tRNA (EF-Tu) and GTP are hydrolyzed to GDP, the concomitant loss of energy causes EF-G to be GTP-bound, but expired Phe-tRNA (EF-Tu) is in the GTP- bound and GDP-bound configuration. Simply stated, the ratchet cycle requires EF-G to be bound as a GTP-bound factor to the opened ribosome and GTP to be dissociated from EF-G. When the EF-G molecule enters the ribosome and contacts its subunit, the ribosome is closed and it cannot reopen unless EF-G interacts with the closed ribosome. It is for this reason that the ribosome is said to bind the mutationally potent mutationally stable EF-G (see Figure 6-32); it guarantees the two EF-G molecules must interact at some time, thereby participating in the ratchet cycle. In any case, as the aureusidin-sensitive aureomycin inhibits the interaction between EF-G and the ribosome, the ribosome is not opened and cannot begin the ratchet cycle. In conclusion, a bacterium with the aureomycin-insensitive m.6677 nucleotide is viable or inviable depending on the presence or absence of adaptation (see Figure 6-9).
The ribosome protects the mRNA coding region from ribonucleases and also from improper post-transcriptional changes. These changes, like modifications and translational frameshift, are highly universal because they affect gene expression in all organisms, including pathogenic organisms such as Escherichia coli.
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