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Nuclear localization of eukaryotic class II release factor (eRF3): Implication for the multifunction of eRF3 in ciliates Euplotes cell
Author(s) -
Chai Baofeng,
Wang Wei,
Liang Aihua
Publication year - 2008
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1016/j.cellbi.2007.12.005
Subject(s) - release factor , cytoplasm , microbiology and biotechnology , immunoelectron microscopy , biology , ciliate , ribosome , organelle , protein biosynthesis , cell , gene , rna , biochemistry , genetics , antibody
Class II polypeptide release factor (eRF3), a ribosome and eRF1‐dependent GTPase, is an important factor, which acts cooperatively with eRF1 to promote hydrolysis of the ester bond linking the polypeptide chain with the peptidyl site tRNA in process of termination of protein synthesis. We prepared antibodies against eRF3 of Euplotes octocarinatus , and performed localization studies by immunoelectron microscopy in the ciliate. Our results indicate that eRF3 is present both in the cytoplasm and the two types of nuclei of this organism. The functions of eRF3 in these nuclei were analyzed by RNA interference methods. The nuclei loose their shape in eRF3 gene‐interfered Euplotes cells, suggesting that eRF3 is probably involved in the morphological organization of nuclei. This suggests that eRF3 is a multifunctional protein with roles additionals to its function in the process of termination of protein synthesis.