A Database of Drosophila Genes & Genomes

FB2013_03, released May 7th, 2013
 

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Citation Hudry, B., Viala, S., Graba, Y., Merabet, S. (2011). Visualization of protein interactions in living Drosophila embryos by the bimolecular fluorescence complementation assay.  BMC Biol. 9(): 5. (Export to RIS)
FlyBase ID FBrf0213066
Publication Type Research paper
PubMed ID 21276241
PubMed Abstract Protein interactions control the regulatory networks underlying developmental processes. The understanding of developmental complexity will, therefore, require the characterization of protein interactions within their proper environment. The bimolecular fluorescence complementation (BiFC) technology offers this possibility as it enables the direct visualization of protein interactions in living cells. However, its potential has rarely been applied in embryos of animal model organisms and was only performed under transient protein expression levels.Using a Hox protein partnership as a test case, we investigated the suitability of BiFC for the study of protein interactions in the living Drosophila embryo. Importantly, all BiFC parameters were established with constructs that were stably expressed under the control of endogenous promoters. Under these physiological conditions, we showed that BiFC is specific and sensitive enough to analyse dynamic protein interactions. We next used BiFC in a candidate interaction screen, which led to the identification of several Hox protein partners.Our results establish the general suitability of BiFC for revealing and studying protein interactions in their physiological context during the rapid course of Drosophila embryonic development.
DOI 10.1186/1741-7007-9-5
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Language of Publication English
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Publication Type Journal
Abbreviation BMC Biol.
Title BMC Biology
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ISBN/ISSN 1741-7007
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