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.
journal_name
Nat Biotechnoljournal_title
Nature biotechnologyauthors
Hu CD,Kerppola TKdoi
10.1038/nbt816subject
Has Abstractpub_date
2003-05-01 00:00:00pages
539-45issue
5eissn
1087-0156issn
1546-1696pii
nbt816journal_volume
21pub_type
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