DOI: 10.1073/pnas.69.3.752. Elongation Factors EF Tu and EF G Interact at Related Sites on Ribosomes

Elongation Factors EF Tu and EF G Interact at Related Sites on Ribosomes

10.1073/pnas.69.3.752

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

The binding of elongation factor EF G to ribosomes inhibits the subsequent reaction of the ribosomes with the ternary complex aminoacyl-tRNA·EF Tu·GTP. Both the hydrolysis of GTP and the binding of aminoacyl-tRNA to ribosomes are nearly abolished by the previous binding of factor EF G to ribosomes in the presence of either fusidic acid plus either GTP or a nonhydrolyzable analog of GTP. The results suggest that each elongation factor binds to the same region on the ribosome. The GTPase activities of both factors EF G and EF Tu may be activated by interaction at the same ribosomal site, as has been previously suggested by others.

Bibliography

Miller, D. L. (1972). Elongation Factors EF Tu and EF G Interact at Related Sites on Ribosomes. Proceedings of the National Academy of Sciences, 69(3), 752â755.

Authors 1

David Lee Miller (first)

References 0 Referenced 63

None

Dates

Type	When
Created	19 years, 2 months ago (May 31, 2006, 2:33 a.m.)
Deposited	3 years, 4 months ago (April 13, 2022, 10:37 a.m.)
Indexed	2 months ago (June 26, 2025, 5:29 a.m.)
Issued	53 years, 5 months ago (March 1, 1972)
Published	53 years, 5 months ago (March 1, 1972)
Published Online	53 years, 5 months ago (March 1, 1972)
Published Print	53 years, 5 months ago (March 1, 1972)

Funders 0

None

BibTeX

@article{Miller_1972, title={Elongation Factors EF Tu and EF G Interact at Related Sites on Ribosomes}, volume={69}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.69.3.752}, DOI={10.1073/pnas.69.3.752}, number={3}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Miller, David Lee}, year={1972}, month=mar, pages={752–755} }

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