Expression, characterization and immunolocalization of translation termination factor eRF3 in the ciliate Euplotes octocarinatus

Class II polypeptide release factor eRF3 stimulates translation termination in a GTP-dependent manner. Recent data show that eRF3 is also involved in cell cycle regulation apart from its function in translation. Here we show that recombinant Eo-eRF3 from the ciliate Euplotes octocarinatus expressed...

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Bibliographic Details
Published in:Research in microbiology 2006-04, Vol.157 (3), p.235-240
Main Authors: Chai, Bao-feng, Wang, Wei, Liang, Ai-hua
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Codon, Nonsense
Cytoskeleton
Escherichia coli
Escherichia coli - metabolism
Euplotes - metabolism
Euplotes - ultrastructure
Euplotes octocarinatus
Fundamental and applied biological sciences. Psychology
GTPase activity
Immunohistochemistry
Immunolocalization
Microbiology
Microscopy, Electron, Transmission
Mutation
Peptide Termination Factors - genetics
Peptide Termination Factors - metabolism
Polypeptide release factor 3
Protein Biosynthesis
Recombinant Proteins - metabolism
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Summary:Class II polypeptide release factor eRF3 stimulates translation termination in a GTP-dependent manner. Recent data show that eRF3 is also involved in cell cycle regulation apart from its function in translation. Here we show that recombinant Eo-eRF3 from the ciliate Euplotes octocarinatus expressed in Escherichia coli can be tested for its ribosome-dependent GTPase activity using an in vitro system. Moreover, polyclonal antibodies against recombinant Eo-eRF3 were used to determine the localization of Eo-eRF3 using immunofluorescence and immunoelectron microscopy, which showed that the Eo-eRF3 is distributed not only around the macronucleus, but also in basal bodies in the cortex of E. octocarinatus cells. The results suggest that Eo-eRF3 may be involved in cytoskeleton organization in addition to its function in translation termination.
ISSN:0923-2508
1769-7123
DOI:10.1016/j.resmic.2005.08.001