Elongation factor G-dependent binding of a photoreactive GTP analogue to Escherichia coli ribosomes results in labeling of protein L11.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference29 articles.
1. Movement of the ribosome along the messenger ribonucleic acid during protein synthesis
2. Studies on translocation. 21. Steady state kinetic analysis of the mechanism of guanosine triphosphate hydrolysis catalyzed by Escherichia coli elongation factor G and the ribosome
3. Studies on translocation. 22. Equilibrium measurements of the interactions of guanine nucleotides with Escherichia coli elongation factor G and the ribosome
4. Function of sulfhydryl groups in ribosome-elongation factor G reactions. Assignment of guanine nucleotide binding site to elongation factor G.
5. The involvement of 50S ribosomal protein L11 in the EF-G dependent GTP hydrolysis ofE. coliribosomes
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