Chemical Cross‐Linking of Elongation Factor G to both Subunits of the 70‐S Ribosomes from Escherichia coli
- 1 October 1982
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 127 (2) , 225-229
- https://doi.org/10.1111/j.1432-1033.1982.tb06859.x
Abstract
Ribosomal proteins situated at or near the binding site of elongation factor G (EF-G) on the E. coli ribosome were 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 .cntdot. 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. EF-G is probably bound close to the ribosomal subunit interface.This publication has 27 references indexed in Scilit:
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