Fig. 2: Scc2-Scc4 binds the RSC ATPase domain. | Nature Communications

Fig. 2: Scc2-Scc4 binds the RSC ATPase domain.

From: Functional crosstalk between the cohesin loader and chromatin remodelers

Fig. 2

a Schematic representing Sth1 domain architecture and the Sth1365–1097 construct (CLMS, cross linking mass spectrometry; HSA, helicase-SANT-associated; SnAc, Snf2 ATP coupling domains). The positions of the CLMS contact and peptide array interactions are indicated. b Interaction between Scc2-Scc4 and Sth1365–1097. Equimolar amounts of cohesin loader and either the RSC complex or Sth1365–1097 were mixed, followed by cohesin loader immunoprecipitation (IP). Sth1 coprecipitation was analyzed by immunoblotting. c Sth1365–1097 interaction with Scc2-Scc4 (2-4), Scc2C (2C) or Scc4-Scc2N (4-2 N), coupled to anti-HA antibody-coated magnetic beads. Recovered protein was visualized by Coomassie Blue staining. * Asterisks indicate heavy and light chains of the antibody used for immunoprecipitation. d Preferential interaction in a nucleotide-bound state. Immunoprecipitation experiments in c were repeated in the presence of either ATP or ADP・BeF3. The experiments shown in panels bd were twice repeated with similar results. Source data are provided as a Source Data file.

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