ИСТИНА

Protein eRF1 (437 a.a., 50 kDa) plays a key role in the process of eukaryotic translation termination. It consists of three structurally and functionally distinct domains: N-terminal domain is responsible for the stop-codon recognition, middle-domain participates in the release of the nascent peptide and C-domain is involved in the regulation of the translation termination. Termination of the protein biosynthesis has been thoroughly investigated, however, the structure and dynamical behavior of the full-length eRF1 in solution remains to be unclear. Here we present solution NMR and molecular dynamic study of the 50 kDa protein eRF1. Assignment for back-bone atoms has been obtained. Remarkable chemical shift difference has been observed for several residues in the full-length protein as compared to those in isolated domains. Molecular dynamic has been implemented to interpret these findings. Acknowledgements This work was supported by the Russian Science Foundation (grant 14-14-00598). Molecular dynamic simulation has been accomplished on supercomputer Lomonosov at Moscow State University supercomputing center.