Figure 2 : TetR fusion proteins enhance translational regulation in both S. cerevisiae and P. falciparum.

From: Synthetic RNA–protein modules integrated with native translation mechanisms to control gene expression in malaria parasites

Figure 2

(a) In S. cerevisiae, various proteins fused to TetR were evaluated for their ability to enhance doxycycline-dependent regulation of a vYFP reporter via either five or ten tandem TetR aptamers positioned within the 3′-UTR. (b) In P. falciparum, regulated expression of a FLuc reporter by TetR and the TetR-DOZI fusion was tested. Three reporter contexts were examined, namely: (i) single TetR aptamer in the 5′-UTR only; (ii) single mutated TetR aptamer in the 5′-UTR and 10 × TetR aptamers in the 3′-UTR; and (iii) single TetR aptamer in the 5′-UTR and 10 × TetR aptamers in the 3′-UTR. Functional and mutated (no binding to TetR) aptamers are illustrated as green and red lollipops, respectively. In both panels, fold induction is calculated as the ratio of reporter expression in the induced state (+aTc) relative to that in the repressed state (−aTc). Data shown are the mean±s.d. from biological triplicates, and are representative of two (S. cerevisae) and three (P. falciparum) independent experiments. *P<0.05; ***P<0.0001 by t-test. NS=Not significant.