Fig. 7
Characterization of interaction distances by integration of MAC-tag data. a–c Distance based topology of protein complexes. The AP-MS and BioID data was blotted based on the bait normalized prey abundances and the correlated data was used to derive interaction distances for CDK7 and the TFIIH complex, as well as for CDK8 and MED13 with the Mediator complex. The CDK7 formed CAK-complex components are shown in gray and the Mediator complex components assigned to the Head (magenta), the Middle (cyan) and the Tail (green) are color-coded. d, e The derived interaction distances for CDK7, CDK8 and the MED13 are fitted into EM derived complex structures and suggested fitted interaction surface is shown in green dashed line ellipses. The color-coding in e corresponds with b, c. f Relative distances for bait protein and the other complex components can be calculated. (g, h) The calculated relative distances (using either PSM or MS1 intensity values) derived from the integrated AP-MS and BioID data results to extremely high correlation (Pearson’s and Spearman’s) and p-value as indicated (t-test) for CDK8 and MED13, two neighboring units in the Mediator kinase module
