Abstract
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 · 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.
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Dates
Type | When |
---|---|
Created | 20 years, 5 months ago (March 3, 2005, 5:15 p.m.) |
Deposited | 1 year, 9 months ago (Nov. 22, 2023, 3:53 p.m.) |
Indexed | 1 year, 9 months ago (Nov. 22, 2023, 4:17 p.m.) |
Issued | 42 years, 10 months ago (Oct. 1, 1982) |
Published | 42 years, 10 months ago (Oct. 1, 1982) |
Published Online | 20 years, 5 months ago (March 3, 2005) |
Published Print | 42 years, 10 months ago (Oct. 1, 1982) |
@article{SK_LD_1982, title={Chemical Cross‐Linking of Elongation Factor G to both Subunits of the 70‐S Ribosomes from Escherichia coli}, volume={127}, ISSN={1432-1033}, url={http://dx.doi.org/10.1111/j.1432-1033.1982.tb06859.x}, DOI={10.1111/j.1432-1033.1982.tb06859.x}, number={2}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={SKÖLD, Sven‐Erik}, year={1982}, month=oct, pages={225–229} }