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- _6 value "To confirm that the coactivation of MEF2C by PGC-1? observed in reporter gene assays (Fig. 3B) was linked to direct binding of these two proteins, we tested whether PGC-1? directly interacts with MEF2C on this MEF-binding site. Increasing amounts of PGC-1? protein (amino acids 31?797) decreased the mobility of the complex containing MEF2C bound to the MEF-binding site, as visualized by a supershift in electrophoretic mobility-shift assays (Fig. 3D). As a control, PGC-1? protein that lacks the MEF2C-interaction domain (amino acids 1?180; see ref. 7) was not able to bind to MEF2C. Inclusion of an MEF2- specific antibody was able to supershift further the protein?DNA complex containing MEF2C, PGC-1?, and the MEF2-binding site (Fig. 3E). Neither a shift nor a supershift could be obtained when using the mutated ?MEF site. These results indicate that MEF2s bind to the PGC-1? promoter and that PGC-1? coactivates MEF2 proteins on the PGC-1? promoter by a direct protein?protein interaction." provenance.
- _6 wasQuotedFrom 12764228 provenance.