Domain motions of class I release factor induced by binding with class II release factor from Euplotes octocarinatus
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The binding of both factors (eRF1 and eRF3) is essential for fast kinetics of the termination of protein translation. The C-terminal domain of eRF1 is known to interact with the C domain of eRF3. Eo-eRF1b contains two highly conserved tryptophan residues (W-11 and W-373), W-11 located in the Eo-eRF1b N domain and W-373 located in the EoeRF1b C domain. Fluorimetry was used to study the interactions of the proteins. When binding with Eo-eRF3Cm6, the emission peak of Eo-eRF1b is blue shifted, while the emission peak of Eo-eRF1bC has no notable change. Our results suggest that the eRF1-eRF3 interaction induces the N and C domain of eRF1b to become closer to each other.
Key wordssteady-state fluorescence quenching eRF1-eRF3 interaction Euplotes octocarinatus
class I polypeptide release factor in eukaryotes
class II polypeptide release factor in eukaryotes
class I polypeptide release factor b in Euplotes octocarinatus
N domain of Eo-eRF1b
C domain of Eo-eRF1b
class II polypeptide release factor in E. octocarinatus
truncated peptide of Eo-eRF3 (a.a. 640–723)
heterodimeric complex of Eo-eRF1b and Eo-eRF3Cm6
heterodimeric complex of Eo-eRF1bC and Eo-eRF3Cm6
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