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comparable to the very high concentrations (∼3–30 μM) of themajor tRNA species found in rapidly growing E. coli (31).This concentration scale can be converted to a proteomefraction (φM) of tRNA-affiliated proteins (referred to henceforthas T-proteins). This class of proteins includes EF-Tu and thetRNA synthetases, which are found at constant ratio to EF-Tu inE. coli (15). Considering the protein mass of EF-Tu and tRNAsynthetases, we obtain a scale of φM ≈ 0.02. This is consistentwith the measured proteome fraction of T-proteins in the cell,which ranges between 5% and 13% depending on growth conditionsand corresponds to ∼60% of the ribosomal protein mass(Fig. 1A). As the estimated Michaelis constant corresponds tothe concentration at which translation would proceed at half ofits maximal speed, these numbers indicate that the translationspeed ranges between 70% and 86% of its maximum, consistentwith earlier estimates for Salmonella (16). Our estimate of theMichaelis constant thus suggests that translation indeed operatesclose to the diffusion limit and that macromolecular crowdingimposes a substantial cost to the cell by setting a large scale forthe required allocation of T-proteins.
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