Galactosidase protein complementation assays

The fl-galactosidase complementation assay has also been adapted for use in mammalian cells (Rossi et al., 1997). The availability of fluorescent substrates for (3-galactosidase allows for fluorescence microscopy and FACS analysis of mammalian cells expressing the fusion proteins of interest. Therefore, similar to the mDHFR system, fl-galactosidase complementation assays may prove useful for genome-scale studies of protein-protein interactions in mammalian cells. 

Rossi F, Charlton CA, Blau HM. Monitoring protein-protein interactions in intact eukaryotic cells by beta-galactosidase complementation. Proc. Natl. Acad. Sci. U.S.A. 1997 94 8405-8410. Wehrman TS, Casipit CL, Gewertz NM, Blau HM. Enzymatic detection of protein translocation. Nat. Methods 2005 2 521-527. Hammer MM, Wehrman TS, Blau HM. A novel enzyme complementation-based assay for monitoring G-protein-coupled receptor internalization. FASEB J. 2007 21 3827-3834. 

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