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  • Title: Utilizing bimolecular fluorescence complementation (BiFC) to assay protein-protein interaction in plants.
    Author: Ohad N, Yalovsky S.
    Journal: Methods Mol Biol; 2010; 655():347-58. PubMed ID: 20734272.
    Abstract:
    Protein function is often mediated by the formation of stable or transient complexes. Here we present a method for testing protein-protein interactions in plants designated bimolecular fluorescence complementation (BiFC). The advantages of BiFC are its simplicity, reliability, and the ability to observe protein-protein interactions in different cellular compartments including membranes. BiFC is based on splitting the yellow fluorescent protein (YFP) into two nonoverlapping N-terminal (YN) and C-terminal (YC) fragments. Each fragment is cloned in-frame with a gene of interest, enabling expression of a fusion protein. Reconstitution of the fluorescing YFP chromophore takes place upon interaction of protein pairs that are coexpressed in the same cells.
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