Share This Author
Structural Basis for the Function of the Ribosomal L7/12 Stalk in Factor Binding and GTPase Activation
Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome
In contrast to current models, EF-G-dependent GTP hydrolysis is shown to precede, and greatly accelerate, the rearrangement of the ribosome that leads to translocation.
EF-P Is Essential for Rapid Synthesis of Proteins Containing Consecutive Proline Residues
- L. Doerfel, Ingo Wohlgemuth, C. Kothe, F. Peske, H. Urlaub, M. Rodnina
- Biology, ChemistryScience
- 4 January 2013
It is shown that EF-P prevents ribosome from stalling during synthesis of proteins containing consecutive prolines, such as PPG, PPP, or longer proline strings, in natural and engineered model proteins.
Kinetic determinants of high-fidelity tRNA discrimination on the ribosome.
Complete kinetic mechanism of elongation factor Tu‐dependent binding of aminoacyl‐tRNA to the A site of the E.coli ribosome
A characteristic feature of the mechanism is the existence of two conformational rearrangements which limit the rates of the subsequent chemical steps of A‐site binding.
Structure of the E. coli ribosome–EF-Tu complex at <3 Å resolution by Cs-corrected cryo-EM
The refined cryo-EM-based model presents the currently most complete high-resolution structure of the E. coli ribosome, which demonstrates the power of cryo -EM in structure determination of large and dynamic macromolecular complexes.
Structural basis for the inhibition of the eukaryotic ribosome
- N. G. D. Loubresse, I. Prokhorova, W. Holtkamp, M. Rodnina, G. Yusupova, M. Yusupov
- Biology, ChemistryNature
- 25 September 2014
X-ray crystallography is used to determine high-resolution structures of 80S ribosomes from Saccharomyces cerevisiae in complexes with 12 eukaryote-specific and 4 broad-spectrum inhibitors, which suggest a model for the action of cycloheximide and lactimidomycin and provide insights into translation inhibitor mode of action.
An elongation factor G-induced ribosome rearrangement precedes tRNA-mRNA translocation.
The ribosome as an entropy trap.
- Annette Sievers, M. Beringer, M. Rodnina, R. Wolfenden
- Chemistry, BiologyProceedings of the National Academy of Sciences…
- 25 May 2004
The results are consistent with the view that the ribosome enhances the rate of peptide bond formation mainly by positioning the substrates and/or water exclusion within the active site, rather than by conventional chemical catalysis.
Ribosome dynamics and tRNA movement by time-resolved electron cryomicroscopy
The structures indicate how tRNA movement is coupled with global and local conformational changes of the ribosome, in particular of the head and body of the small ribosomal subunit, and show that dynamic interactions between tRNAs andribosomal residues confine the path of the tRNAAs through the ribo-EM.