Chemical cross-linking of elongation factor G to both subunits of the 70-S ribosomes from Escherichia coli

Eur J Biochem. 1982 Oct;127(2):225-9. doi: 10.1111/j.1432-1033.1982.tb06859.x.


Ribosomal proteins situated at or near the binding site of elongation factor G (EF-G) on the Escherichia coli ribosome have been identified by use of the bifunctional, cleavable cross-linker, dimethyl-4,9-diaza-5,8-dioxo-6,7-dihydroxy-dodecanebisimidate. Five different bimolecular EF-G x ribosomal-protein complexes were isolated electrophoretically. The ribosomal proteins found in each of these complexes were identified as the 50-S-subunit proteins L6, L7/L12 and L14 and the 30-S-subunit proteins S12 and S19. In the presence of thiostrepton, which prevents binding of EF-G to the ribosome, there was a considerable decrease in the yield of each of these cross-linked complexes. The data suggest that EF-G is bound close to the ribosomal subunit interface.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / isolation & purification*
  • Chemical Phenomena
  • Chemistry
  • Cross-Linking Reagents*
  • Escherichia coli / metabolism*
  • Imidoesters
  • Peptide Elongation Factor G
  • Peptide Elongation Factors / isolation & purification*
  • Protein Binding
  • Ribosomal Proteins / isolation & purification*


  • Bacterial Proteins
  • Cross-Linking Reagents
  • Imidoesters
  • Peptide Elongation Factor G
  • Peptide Elongation Factors
  • Ribosomal Proteins
  • dimethyl-3,8-diaza-4,7-dioxo-5,6-dihydroxydecanbis(imidate)