Fig. 3.
TAF15–CIZ fusion Pazopanib are cleaved in vitro by recombinant caspases-3 and -7. (A) Schematic diagram of TAF15 and oncogenic TAF15–CIZ fusion proteins. TAF15 contains a transactivation domain (SYQG repeats) at the N-terminus, a RNA recognition motif (RRM), a zinc finger (ZF), and a RNA binding domain (RGG) at the C-terminus. CIZ/NMP4 contains leucine-rich (LZ), serine-rich (SR) and proline-rich (PR) domains at the N-terminus, and a nuclear localization signal (NLS), eight Kruppel-type C2H2 zinc fingers (ZF) and a Gln-Ala repeat (QA) at the C-terminus. TAF15–CIZ/NMP4 fusion proteins (S and L forms) encompass various lengths of N-terminal SYQG domain from TAF15, fused in frame to the complete sequence of CIZ/NMP4. The caspase cleavage site is indicated by arrowheads. (B) In vitro translated biotinylayed TAF15–CIZ/NMP4 isoforms were incubated with caspases-3 or -7 for 3 h at 37 °C and immunoblotted by streptavidin–HRP. CIZ/NMP4 is included as a negative control.
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