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. 2011 Oct 3;108(42):17438–17443. doi: 10.1073/pnas.1111855108

Fig. 5.

Fig. 5.

Coprecipitation of the MuvB core complex by Myb WT and mutant proteins. FLAG-tagged Myb WT or mutant protein was expressed in Drosophila S2 cells by transient DNA transfection. RNAi directed against the 5′-UTR was used to knock down endogenous Myb expression. Immunoblots of total extracts (input) or of immunoprecipitated complexes (FLAG-IP) were analyzed using the indicated antibodies. (Left) Analysis of interaction with the MuvB core complex by full-length (WT), N-terminal, or C-terminal Myb. The anti-Myb antibody recognizes the N-terminal repeats of the Myb DNA-binding domain; therefore, it cannot detect the C-terminal mutant (19). A 50-kDa background band detected by anti-FLAG in all FLAG-IP samples is mouse Ig-heavy chain that is released from the anti-FLAG beads used for immunoprecipitation. (Right) Analysis of interaction with the MuvB core complex by WT or the indicated alanine substitution mutants of Myb.