Drosophila Enhancer of Rudimentary Homolog, ERH, Is a Binding Partner of RPS3, RPL19, and DDIT4, Suggesting a Mechanism for the Nuclear Localization of ERH

Figure 2

Western blots probed with anti-LexA, showing that ERH and RPS3 bind to each other and can be coimmunoprecipitated. (a) Requirement of RPS3 for coimmunoprecipitation. This blot shows that RPS3 must be attached to HA in order for the HA antibody to coprecipitate LexA-ERH. (1) Molecular weight markers. These were superimposed from a photograph of the stained gel. (2) Extracts from cells expressing HA-RPS3 and LexA-ERH. (3) Immunoprecipitates of extracts from cells expressing HA-RPS3 and LexA-ERH immunoprecipitated with anti-HA antibody. (4) Extracts from cells expressing HA and LexA-ERH. (5) Immunoprecipitates of extracts from cells expressing HA and LexA-ERH that have been immunoprecipitated with anti-HA antibody. (b) Requirement of ERH for coimmunoprecipitation. This blot shows that ERH must be attached to LexA in order for the HA antibody to coprecipitate LexA and rules out the possibility that RPR3 binds to LexA alone. (1) Extracts from cells expressing HA-RPS3 and LexA. (2) Immunoprecipitates of extracts from cells expressing HA-RPS3 and LexA and immunoprecipitated with anti-HA antibody. (3) Molecular weight markers. These were superimposed from a photograph of the stained gel. Together the two blots show that both RPS3 and ERH are necessary to get coimmunoprecipitation and confirm that RPS3 and ERH are binding partners.

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