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. 2002 Oct 1;21(19):5118–5129. doi: 10.1093/emboj/cdf530

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Copyright © 2002 European Molecular Biology Organization

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graphic file with name cdf530f3a.jpg — Fig. 3. DIAP1 binding is mediated by the N-terminal IBMs of Jafrac2 and Rpr. (A) AKP- but not KP-Jafrac2 interacts with DIAP1. Co-purification of Jafrac2 with DIAP1 from cellular extracts. In this and subsequent figures, expression and purification of the indicated constructs was determined as in Figure 1D. (B) The thioredoxin peroxidase activity of Jafrac2 is not required for DIAP1 binding. Co-purification of wild-type and Jafrac2 mutants with DIAP1 from cellular extracts. (C) AKP-Jafrac2 directly interacts with DIAP1. In vitro co-purification of recombinant AKP- and KP-Jafrac2 with recombinant DIAP1 protein is shown. First and second panel: immunoblot analysis of Jafrac2- and DIAP1-specific antibodies. Third panel: Coomassie-stained gel of recombinant AKP- and KP-Jafrac2.

graphic file with name cdf530f3b.jpg — Fig. 3. DIAP1 binding is mediated by the N-terminal IBMs of Jafrac2 and Rpr. (A) AKP- but not KP-Jafrac2 interacts with DIAP1. Co-purification of Jafrac2 with DIAP1 from cellular extracts. In this and subsequent figures, expression and purification of the indicated constructs was determined as in Figure 1D. (B) The thioredoxin peroxidase activity of Jafrac2 is not required for DIAP1 binding. Co-purification of wild-type and Jafrac2 mutants with DIAP1 from cellular extracts. (C) AKP-Jafrac2 directly interacts with DIAP1. In vitro co-purification of recombinant AKP- and KP-Jafrac2 with recombinant DIAP1 protein is shown. First and second panel: immunoblot analysis of Jafrac2- and DIAP1-specific antibodies. Third panel: Coomassie-stained gel of recombinant AKP- and KP-Jafrac2.