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Zenodo
2025
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| Online Access: | https://doi.org/10.5281/zenodo.15384259 |
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| _version_ | 1866901917379067904 |
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| author | Hofmann, Jennifer Yang, Theodore Sunol, Alp Zia, Roseanna |
| author_facet | Hofmann, Jennifer Yang, Theodore Sunol, Alp Zia, Roseanna |
| contents | <p>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 <em>Escherichia coli</em> due to competitive combinatoric searching through crowded cytoplasm by thousands of <em>E. coli</em>'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 <em>E. coli</em>. Variable L12 copy numbers may thus have evolved for fast or slow bacterial growth as complementary survival strategies. </p> |
| format | Recurso digital |
| id | zenodo_https___doi_org_10_5281_zenodo_15384259 |
| institution | Zenodo |
| language | |
| publishDate | 2025 |
| publisher | Zenodo |
| record_format | zenodo |
| spellingShingle | Dataset for: Ribosomal L12 stalks recruit elongation factors to speed protein synthesis in Escherichia coli Hofmann, Jennifer Yang, Theodore Sunol, Alp Zia, Roseanna <p>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 <em>Escherichia coli</em> due to competitive combinatoric searching through crowded cytoplasm by thousands of <em>E. coli</em>'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 <em>E. coli</em>. Variable L12 copy numbers may thus have evolved for fast or slow bacterial growth as complementary survival strategies. </p> |
| title | Dataset for: Ribosomal L12 stalks recruit elongation factors to speed protein synthesis in Escherichia coli |
| url | https://doi.org/10.5281/zenodo.15384259 |