C-Myc-Tag Antibody - #T0001

Figure 2. Mtf2 and Sls1 are required for the assembly of Mrh5C.A and B, loss of Mtf2 disrupts Mrh5C. Mitochondrial extracts prepared from WT cells expressing untagged Sls1 (negative control) or Sls1-FLAG (positive control), and Δmtf2 cells expressing Sls1-FLAG were subjected to anti-FLAG co-immunoprecipitation (A). Mitochondrial extracts prepared from WT cells expressing untagged Mrh5 or Mrh5-Myc, and Δmtf2 cells expressing Mrh5-Myc were subjected to anti-Myc co-immunoprecipitation (B). C, loss of Sls1 disrupts Mrh5C. WT cells expressing untagged Mrh5 or Mrh5-Myc and Δmtf2 cells expressing Mrh5-Myc were subjected to anti-Myc co-immunoprecipitation. D, loss of Mrh5 does not affect interactions among other members of Mrh5C. WT cells expressing untagged Sls1 or Sls1-FLAG, and Δmrh5 cells expressing Sls1-FLAG were subjected to anti-FLAG co-immunoprecipitation. E, loss of Ppr4 does not affect interactions among other members of Mrh5C. WT cells expressing untagged Sls1 or Sls1-FLAG, and Δppr4 cells expressing Sls1-FLAG were subjected to anti-FLAG co-immunoprecipitation. F, Mtf2 and Sls1 form a complex independently of Mrh5 and Ppr4. WT cells expressing untagged Sls1 or Sls1-FLAG, and Δmrh5Δppr4 cells expressing Sls1-FLAG were subjected to anti-FLAG co-immunoprecipitation. Mitochondrial extracts (IN) and immunoprecipitates (IP) were analyzed by immunoblotting using specific anti-tag Abs. Genes encoding the Mrh5C subunits were endogenously tagged to facilitate their detection.

Figure 2| Characterization of the binding domains between the NDV M protein and chBRD2 protein. B Mapping the binding domain of the chBRD2 protein for the NDV M protein. Upper panel, schematic representation of the full-length and truncation mutants of the Myc-tagged chBRD2 protein. Lower panel, Myc-tagged chBRD2 or its truncation mutants (Input) interacting with HA-M was detected by western blot.