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Figure 5.
Figure 5. Molecular mechanism of the removal of DIAP1-mediated
Dronc ubiquitination by the pro-apoptosis protein Hid. (a)
The BIR2 domain is required for the ubiquitination of Dronc in
vitro. Various DIAP1 fragments were examined for their E3
ubiquitin ligase activity in the ubiquitination reaction of
Dronc (C318A). The gel was blotted using an anti-Dronc raised
against its CARD domain. E1, E2, Dronc (C318A) and DIAP1 were
individually purified to homogeneity as described in Methods.
(b) A ten-residue peptide derived from the N terminus of Hid
specifically removes DIAP1-mediated ubiquitination of Dronc. The
control peptide has the sequence N-DYPDQNRRRIGAEK-C.
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