Backbone (1)H, (13)C and (15)N resonance assignments of the human eukaryotic release factor eRF1.
Eukaryotic translation termination is mediated by two interacting release factors, eukaryotic class 1 release factor (eRF1) and eukaryotic class 3 release factor (eRF3), which act cooperatively to ensure efficient stop codon recognition and fast polypeptide release. eRF1 consisting of three well-defined functional domains recognizes all three mRNA stop codons located in the A site of the small ribosomal subunit and triggers hydrolysis of the ester bond of peptidyl-tRNA in the peptidyl transfer center of the large ribosomal subunit. Nevertheless, various aspects of molecular mechanism of translation termination in eukaryotes remain unclear. Elucidation of the structure and dynamics of eRF1 in solution is essential for understanding molecular mechanism of its function in translation termination. To approach this problem, here we report NMR backbone signal assignments of the human eRF1 (437 a.a., 50 kDa).
Center for Magnetic Tomography and Spectroscopy, Faculty of Fundamental Medicine, M.V. Lomonosov Moscow State University, Moscow, 119991, Russia, vpolsha@mail.ru.
Vladimir I
VI
Polshakov
Boris D
BD
Eliseev
Ludmila Yu
LY
Frolova
Chi-Fon
CF
Chang
Tai-huang
TH
Huang
D000595:Amino Acid Sequence; D006801:Humans; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010454:Peptide Termination Factors / Q000737:chemistry*; D017434:Protein Structure, Tertiary
C489002:ETF1 protein, human; D010454:Peptide Termination Factors