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| Title | Gut colonization by Bacteroides requires translation by an EF-G paralog lacking GTPase activity. |
|---|---|
| Journal, issue, pages | EMBO J, Vol. 42, Issue 2, Page e112372, Year 2023 |
| Publish date | Jan 16, 2023 |
 Authors | Weiwei Han / Bee-Zen Peng / Chunyan Wang / Guy E Townsend / Natasha A Barry / Frank Peske / Andrew L Goodman / Jun Liu / Marina V Rodnina / Eduardo A Groisman /   |
| PubMed Abstract | Protein synthesis is crucial for cell growth and survival yet one of the most energy-consuming cellular processes. How, then, do cells sustain protein synthesis under starvation conditions when ...Protein synthesis is crucial for cell growth and survival yet one of the most energy-consuming cellular processes. How, then, do cells sustain protein synthesis under starvation conditions when energy is limited? To accelerate the translocation of mRNA-tRNAs through the ribosome, bacterial elongation factor G (EF-G) hydrolyzes energy-rich guanosine triphosphate (GTP) for every amino acid incorporated into a protein. Here, we identify an EF-G paralog-EF-G2-that supports translocation without hydrolyzing GTP in the gut commensal bacterium Bacteroides thetaiotaomicron. EF-G2's singular ability to sustain protein synthesis, albeit at slow rates, is crucial for bacterial gut colonization. EF-G2 is ~10-fold more abundant than canonical EF-G1 in bacteria harvested from murine ceca and, unlike EF-G1, specifically accumulates during carbon starvation. Moreover, we uncover a 26-residue region unique to EF-G2 that is essential for protein synthesis, EF-G2 dissociation from the ribosome, and responsible for the absence of GTPase activity. Our findings reveal how cells curb energy consumption while maintaining protein synthesis to advance fitness in nutrient-fluctuating environments. |
 External links | EMBO J / PubMed:36472247 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.0 - 4.0 Å |
| Structure data | EMDB-27535, PDB-8dmf:  EMDB-27543: One class of E. coli ribosome associated with Bacteroides thetaiotaomicron EF-G2  EMDB-27546: Another class of E. coli ribosome associated with Bacteroides thetaiotaomicron EF-G2  EMDB-27547: Cryo-EM structure of E. coli ribosome associated with Bacteroides thetaiotaomicron EF-G2 from focused 3D refinement  EMDB-27561: E. coli ribosome associated with Bacteroides thetaiotaomicron EF-G2 from combined data |
| Chemicals |  ChemComp-MG:  ChemComp-GTP: |
| Source |
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 Keywords |  TRANSLATION / Translation elongation factor / Bacteroides thetaiotaomicron EF-G2 |
