Crossref journal-article
Wiley
European Journal of Biochemistry (311)
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.

Bibliography

SKÖLD, S. (1982). Chemical Cross‐Linking of Elongation Factor G to both Subunits of the 70‐S Ribosomes from Escherichia coli. European Journal of Biochemistry, 127(2), 225–229. Portico.

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)
Funders 0

None

@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} }