Interactions of N-CoR with mSin3A and TFIIB. (A) Interaction between N-CoR and mSin3A. Radiolabeled N-CoR, synthesized by in vitro transcription and translation, was tested for the ability to bind to GST fusions representing various domains of mSin3A or to nonrecombinant GST, as indicated above the lanes. Radiolabeled N-CoR bound to each GST construct was eluted with soluble glutathione, resolved by SDS-PAGE, and visualized and quantified by PhosphorImager analysis. The percentage of N-CoR bound in each assay is depicted below the lanes, and was determined relative to the total radiolabeled N-CoR used in the assay (input). (B) Interaction between N-CoR and TFIIB. The same protocol as in panel A was employed, but with a GST-TFIIB construct.