Marina V. Rodnina
Max Planck Society
271 Papers
2K Citations
Marina V. Rodnina is an academic researcher from Max Planck Society. The author has contributed to research in topics: Ribosome & Transfer RNA. The author has an hindex of 78, co-authored 242 publications. Previous affiliations of Marina V. Rodnina include Institute of Molecular Biology and Genetics of NASU & Witten/Herdecke University.
Chat about Author
Papers
Interaction of helix D of elongation factor Tu with helices 4 and 5 of protein L7/12 on the ribosome.
TL;DR: It is suggested that helix D of EF-Tu is involved in an initial transient contact with helices 4 and 5 of L7/12 that promotes ternary complex binding to the ribosome.
Fluctuations between multiple EF-G-induced chimeric tRNA states during translocation on the ribosome
Sarah Adio,T. Senyushkina,Frank Peske,N. Fischer,Wolfgang Wintermeyer,Marina V. Rodnina +5 more
TL;DR: Single-molecule FRET is used to follow tRNA translocation in real time, identifying new chimeric intermediates and suggesting how EF-G binding and GTP hydrolysis change the energetic landscape of translocation to accelerate forward tRNA movement.
Spontaneous reverse movement of mRNA-bound tRNA through the ribosome
Andrey L. Konevega,Niels Fischer,Yuri P. Semenkov,Holger Stark,Wolfgang Wintermeyer,Marina V. Rodnina +5 more
TL;DR: It is shown that, in the absence of EF-G, there is spontaneous backward movement, or retrotranslocation, of two tRNAs bound to mRNA, which lends support to the diffusion model of tRNA movement during translocation.
Distortion of tRNA upon Near-cognate Codon Recognition on the Ribosome
TL;DR: The timing and extent of the rearrangement is similar on cognate and near-cognate codons, suggesting that the tRNA distortion alone does not provide a specific switch for the preferential activation of GTP hydrolysis on the cognate codon.
Conformationally restricted elongation factor G retains GTPase activity but is inactive in translocation on the ribosome.
TL;DR: These results strongly argue against a GTPase switch-type model of EF-G function and demonstrate that conformational mobility is an absolute requirement for EF- G function on the ribosome.