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J Mol Biol. 2015 Jun 5;427(11):2039-2055. doi: 10.1016/j.jmb.2015.03.005. Epub 2015 Mar 12.

Bimolecular Fluorescence Complementation (BiFC) Analysis: Advances and Recent Applications for Genome-Wide Interaction Studies.

Author information

1
Molecular Cellular Developmental Biology Program, Ohio State University, OH, USA.
2
Department of Biological Sciences, Seoul National University, Seoul 151-747, Korea.
#
Contributed equally

Abstract

Complex protein networks are involved in nearly all cellular processes. To uncover these vast networks of protein interactions, various high-throughput screening technologies have been developed. Over the last decade, bimolecular fluorescence complementation (BiFC) assay has been widely used to detect protein-protein interactions (PPIs) in living cells. This technique is based on the reconstitution of a fluorescent protein in vivo. Easy quantification of the BiFC signals allows effective cell-based high-throughput screenings for protein binding partners and drugs that modulate PPIs. Recently, with the development of large screening libraries, BiFC has been effectively applied for genome-wide PPI studies and has uncovered novel protein interactions, providing new insight into protein functions. In this review, we describe the development of reagents and methods used for BiFC-based screens in yeast, plants, and mammalian cells. We also discuss the advantages and drawbacks of these methods and highlight the application of BiFC in large-scale studies.

KEYWORDS:

bimolecular fluorescence complementation (BiFC) analysis; fluorescent proteins; genomics; proteomics

PMID:
25772494
PMCID:
PMC4417415
DOI:
10.1016/j.jmb.2015.03.005
[Indexed for MEDLINE]
Free PMC Article
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