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Updated: Jul 7, 2026

Heterokaryon Technique for Analysis of Cell Type-specific Localization
Published on: March 11, 2011
Nuclear localization of eukaryotic class II release factor (eRF3): implication for the multifunction of eRF3 in
Baofeng Chai1, Wei Wang, Aihua Liang
1Institute of Biotechnology, Key Laboratory of Chemical Biology and Molecular Engineering of the Ministry of Education, Shanxi University, Taiyuan 030006, PR China.
Abstract:
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.
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