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

NMR solution structure and function of the C-terminal domain of eukaryotic class 1 polypeptide chain release factor

Termination of translation in eukaryotes is triggered by two polypeptide chain release factors, eukaryotic class 1 polypeptide chain release factor (eRF1) and eukaryotic class 2 polypeptide chain release factor 3. eRF1 is a three-domain protein that interacts with eukaryotic class 2 polypeptide chain release factor 3 via its C-terminal domain (C-domain). The high-resolution NMR structure of the...

NMR assignments of the C-terminal domain of human polypeptide release factor eRF1.

We report NMR assignments of the protein backbone of the C-terminal domain (163 a.a.) of human class 1 translation termination factor eRF1. It was found that several protein loop residues exist in two slowly interconverting conformational states.

1 H , 13 C , and 15 N resonance assignments for the tandem PHD finger motifs of human CHD 4 Louise

The plant homeodomain (PHD) zinc finger is a structural motif of about 40–60 amino acid residues found in many eukaryotic proteins that are involved in chromatinmediated gene regulation. The human chromodomain helicase DNA binding protein 4 (CHD4) is a multi-domain protein that harbours, at its N-terminal end, a pair of PHD finger motifs (dPHD) connected by a *30 amino acid linker. This tandem ...

Two-step model of stop codon recognition by eukaryotic release factor eRF1

Release factor eRF1 plays a key role in the termination of protein synthesis in eukaryotes. The eRF1 consists of three domains (N, M and C) that perform unique roles in termination. Previous studies of eRF1 point mutants and standard/variant code eRF1 chimeras unequivocally demonstrated a direct involvement of the highly conserved N-domain motifs (NIKS, YxCxxxF and GTx) in stop codon recognitio...

(1)H, (15)N and (13)C backbone resonance assignments of the Kelch domain of mouse Keap1