ArticleCommunications biology2025
Ribosomal L12 stalks recruit elongation factors to speed protein synthesis in Escherichia coli.
Article in Communications biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Mapping the architecture of protein complexes inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Stoichiometry-induced differential selection on codon optimization among ribosomal protein genes in bacterial species.Molecular biology and evolution · 2026Article
- Abundant positively-charged proteins underlie JCVI-Syn3A's expanded nucleoid and ribosome distribution.PLoS computational biology · 2026Article
- Ribosomal L12 stalks recruit elongation factors to speed protein synthesis in Escherichia coli.Communications biology · 2025Article
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Authors and funding
4 authors.
Funding
Abstract
Translating ribosomes must wait after each elongation step for a new ternary complex (EF-Tu ⋅ aa-tRNA ⋅ 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. coli's 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.
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