Efficiency of protein synthesis inhibition depends on tRNA and codon compositions
Fig 1
Ribosome and EF-Tu as targets for protein synthesis inhibition.
After a tRNA (gray sphere) is released from a ribosome (gray dome), it binds to an aminoacyl-tRNA synthetase (violet box) that recharges the tRNA with its cognate amino acid (green sphere). Under physiological conditions, the recharged tRNA binds to elongation factor EF-Tu (blue sphere) to form a ternary complex that delivers its amino acid to a translating ribosome. If EF-Tu gets inhibited, e.g., by an antibiotic or toxin, it is no longer able to bind aminoacylated tRNAs (A). Alternatively, protein synthesis and, thus, cellular growth can be impeded through ribosome inhibition (B) or via simultaneous inhibition of ribosomes and EF-Tu (C). See Table 1 for more details on the different inhibition pathways.