Backbone 1H, 13C and 15N resonance assignments of the human eukaryotic release factor eRF1

Vladimir I. Polshakov*, Boris D. Eliseev, Ludmila Yu Frolova, Chi Fon Chang, Tai huang Huang

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


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).

Original languageEnglish
Pages (from-to)37-42
Number of pages6
JournalBiomolecular NMR Assignments
Issue number1
Publication statusPublished - 2015 Apr
Externally publishedYes


  • Human polypeptide release factor eRF1
  • NMR assignments
  • Protein domains
  • Termination of protein synthesis

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry


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