TY - JOUR
T1 - Backbone 1H, 13C and 15N resonance assignments of the human eukaryotic release factor eRF1
AU - Polshakov, Vladimir I.
AU - Eliseev, Boris D.
AU - Frolova, Ludmila Yu
AU - Chang, Chi Fon
AU - Huang, Tai huang
PY - 2015/1/1
Y1 - 2015/1/1
N2 - 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).
AB - 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).
KW - Human polypeptide release factor eRF1
KW - NMR assignments
KW - Protein domains
KW - Termination of protein synthesis
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U2 - 10.1007/s12104-014-9540-8
DO - 10.1007/s12104-014-9540-8
M3 - Article
C2 - 24452424
AN - SCOPUS:84892567450
VL - 9
SP - 37
EP - 42
JO - Biomolecular NMR Assignments
JF - Biomolecular NMR Assignments
SN - 1874-2718
IS - 1
ER -