Green fluorescent protein reduction

Kummer AD, Kompa C, Lossau H, Pollinger-Dammer F, Michel-Beyerle ME, Silva CM, Bylina EJ, Coleman WJ, Yang MM, Youvan DC (1998) Dramatic reduction in fluorescence quantum yield in mutants of green fluorescent protein due to fast internal conversion. Chem Phys 237 183-193... 

Index Entries Green fluorescent protein thermal stability decimal reduction time three-phase partitioning fluorescence intensity acetate phosphate. 

More recently Michnick and co-workers have introduced a dihydrofolate reductase complementation system, which seems to be particularly robust [61 - 65], They attribute the success of this system to the fact that the N-terminal (1 - 105) and C-terminal (106 - 186) DHFR fragments do not fold until they are dimerized. In addition to the obvious selection for essential metabolites dependent on the reduction of dihydrofolate to tetrahydrofolate, protein-protein interactions are detected based on the retention of a fluorescein-methotrexate conjugate. Several other enzymes have been employed for the design of complementation assays, including green fluorescent protein, which allows screens based on fluorescence or FRET [66 - 68]. As with the bacterial transcription assays, these complementation systems are new. It will be interesting to see if, as the selections are optimized, these systems prove competitive with the Y2H assay. 

Kummer, A.D., Kompa, C., Lossau, H., Pbllinger-Dammer, E, Michel Beyerle, M.E., Silva, C.M., Bylina, E.J., Coleman, W.J., Yang, M.M., and Youvan, D.C., Dramatic reduction in fluorescence quantum yield in mutants of Green Fluorescent Proteins due to fast internal conversion, Chem. Phys., 237, 183-193, 1998. 

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