Fig. 2: DNA-binding activity of p73 is required for its inhibitory effect on Th1 differentiation. | Nature Communications

Fig. 2: DNA-binding activity of p73 is required for its inhibitory effect on Th1 differentiation.

From: Transcription factor p73 regulates Th1 differentiation

Fig. 2

a Schematic of the domain structure of WT and mutant p73 proteins. The transactivation (TA) domain, DNA-binding domain (DBD), oligomerization domain (OD), and sterile α motif (SAM) are indicated. Mutations in two zinc-binding sites (Zn-A* and Zn-B*) are marked as indicated. b Empty vector or different p73 constructs were overexpressed in Th1 cells via retroviral transduction. IFNγ expression levels were determined by intracellular staining and flow cytometric analysis and expressed as the percentage of IFNγ+ cells from different p73 mutant-transduced cells (GFP+). Data represent mean ± S.D. from a total of n = 12 biological replicates over four independent experiments. P values of mutant p73 compared to empty vector were determined by two-tailed unpaired t test. ***P < 0.001. Source data for b are provided in a Source Data File.

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