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TitleCryo-EM structural analyses reveal a unique role for elongation factor G2 (EF-G2) in Mycobacteria.
Journal, issue, pagesFEBS J, Vol. 292, Issue 24, Page 6533-6556, Year 2025
Publish dateJun 26, 2025
AuthorsPriya Baid / Jayati Sengupta /
PubMed AbstractThe gene-encoding translation elongation factor G (EF-G) has undergone gene duplication across various bacterial species including Mycobacteria, and in mammalian mitochondria, leading to the ...The gene-encoding translation elongation factor G (EF-G) has undergone gene duplication across various bacterial species including Mycobacteria, and in mammalian mitochondria, leading to the emergence of the paralogue elongation factor G2 (EF-G2). Our study reveals that mycobacterial EF-G2, unlike EF-G1, neither participates in ribosome-recycling nor significantly contributes to overall translation, suggesting that it plays an alternative role in Mycobacteria. Remarkably, our investigation found a significant overexpression of mycobacterial EF-G2 during the stationary growth phase. Moreover, EF-G2 lacks ribosome-dependent GTPase activity, an observation consistent with previous reports. Cryo-EM analysis of the M. smegmatis 70S ribosome purified from the nutrient-starved (stationary) phase and complexed with EF-G2 unveiled the structural basis for its inability to hydrolyse GTP in a ribosome-dependent manner. Furthermore, we report an unprecedented binding mode of two EF-G2 copies on the 50S ribosomal subunit that impedes subunit association, thereby preventing the formation of active 70S ribosomes. Thus, instead of performing canonical functions, mycobacterial EF-G2 acts as a translation repressor during nutrient starvation. Altogether, our findings shed light on the multifaceted mechanisms by which EF-G2 modulates protein synthesis under nutrient-limited conditions, providing insights into adaptive strategies employed by Mycobacteria to survive in hostile environments.
External linksFEBS J / PubMed:40569974
MethodsEM (single particle)
Resolution3.6 - 4.7 Å
Structure data

61959

9k0z

EMDB-61959, PDB-9k0z:
EF-G2 bound 70S ribosome complex of M. smegmatis
Method: EM (single particle) / Resolution: 4.7 Å

61960

9k10

EMDB-61960, PDB-9k10:
EF-G2 bound 50S ribosome subunit complex of M. smegmatis
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

ChemComp-PHE:
PHENYLALANINE

ChemComp-GNP:
PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / GppNHp, GMPPNP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

Source
  • mycolicibacterium smegmatis mc2 155 (bacteria)
KeywordsRIBOSOME / Mycobacterium 70S ribosome / stationary phase / elongation factor G2 / non-canonical factor / Mycobacterium 50S ribosomal subunit

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