title: Domain motions of class I release factor induced by binding with class II release factor from Euplotes octocarinatus.
abstract: 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 Eo-eRF1b 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.
authors.affiliation: Institute of Biotechnology and Institute of Molecular Science, Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, Shanxi University, Taiyuan 030006, China.
authors.forename: Jie
authors.initials: J
authors.lastname: Chen
authors.forename: Bing-sheng
authors.initials: BS
authors.lastname: Yang
authors.forename: Ai-hua
authors.initials: AH
authors.lastname: Liang
mesh_terms: D016812:Euplotes / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D010454:Peptide Termination Factors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D020033:Protein Isoforms / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: D010454:Peptide Termination Factors; D020033:Protein Isoforms