Pre-loading of translation molecules onto ribosomes speeds transport and protein synthesis in Escherichia coli
Translating ribosomes must wait after each elongation step for a new ternary complex (EF-Tu{middle dot}aa-tRNA{middle dot}GTP) to arrive, facilitating rapid codon recognition testing. We recently showed that this wait-time rate-limits elongation in Escherichia coli due to competitive combinatoric searching through crowded cytoplasm by thousands of E. colis 42 unique ternary complexes. Here, we investigate whether ribosomal L12 subunits pool translation molecules to reduce this wait time. We mimic transport and reactions underlying elongation in a physiologically accurate, physically-resolved model of crowded cytoplasm. We find that L12 pre-loading as much as doubles translation rate by reducing diffusive search time. But more L12 is not always better: faster-growing bacteria tend to have fewer L12. We resolve this apparent contradiction by demonstrating tradeoffs between binding and novel sampling as a function of copy number in E. coli. Variable L12 copy numbers may thus have evolved for fast or slow bacterial growth as complementary survival strategies.