The L7/L12 proteins change their conformation upon interaction of EF‐G with ribosomes
- 15 October 1984
- journal article
- Published by Wiley in FEBS Letters
- Vol. 176 (1) , 32-36
- https://doi.org/10.1016/0014-5793(84)80906-0
Abstract
The different functional complexes of ribosomes with elongation factor F (EF-G) were studied by digestion experiments with trypsin. It was found that upon interaction of EF-G with ribosomes the L7/L12 proteins are sensitive to trypsin and are trypsin resistant after dissociation of EF-G from ribosomes. The significance of conformational alterations in the L7/L12 and also in the other proteins in the translation process is discussed.Keywords
This publication has 18 references indexed in Scilit:
- Elongation factor G protects a nuclease-sensitive site of 23 S RNA within the ribosomeFEBS Letters, 1984
- Structural studies of ribosomesProgress in Biophysics and Molecular Biology, 1982
- Specific interaction of the elongation factor EF‐G with the ribosomal 23 S RNA from Escherichia coliFEBS Letters, 1982
- Proton nuclear magnetic resonance study of the ribosomal protein L7/L12 in situFEBS Letters, 1982
- Localization of the elongation factor g on escherichia coli ribosomeFEBS Letters, 1981
- Elongation factor‐dependent reactions on ribosomes deprived of proteins L7 and L12FEBS Letters, 1977
- Stepwise elongation factor G-promoted elongation of polypeptides on the ribosome without GTP cleavageJournal of Molecular Biology, 1976
- Ribosomal proteins of Escherichia coli. I. Purification of the 30 S ribosomal proteinsBiochemistry, 1969
- Binding of specific sRNA to template ribosome complex: Effect of proteolytic enzymesJournal of Molecular Biology, 1966
- Effect of Trypsin on Escherichia Coli and Rabbit Reticulocyte RibosomesNature, 1966