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Nat Biotechnol. 2003 May;21(5):539-45. Epub 2003 Apr 14.

Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis.

Author information

1
Howard Hughes Medical Institute and Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI 48109-0650, USA.

Abstract

The specificity of biological regulatory mechanisms relies on selective interactions between different proteins in different cell types and in response to different extracellular signals. We describe a bimolecular fluorescence complementation (BiFC) approach for the simultaneous visualization of multiple protein interactions in the same cell. This approach is based on complementation between fragments of fluorescent proteins with different spectral characteristics. We have identified 12 bimolecular fluorescent complexes that correspond to 7 different spectral classes. Bimolecular complex formation between fragments of different fluorescent proteins did not differentially affect the dimerization efficiency of the bZIP domains of Fos and Jun or the subcellular sites of interactions between these domains. Multicolor BiFC enables visualization of interactions between different proteins in the same cell and comparison of the efficiencies of complex formation with alternative interaction partners.

PMID:
12692560
PMCID:
PMC1820765
DOI:
10.1038/nbt816
[Indexed for MEDLINE]
Free PMC Article

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