Fig. 2: Structure of the Taf14ET–Sth1EBM complex determined by NMR. | Nature Communications

Fig. 2: Structure of the Taf14ET–Sth1EBM complex determined by NMR.

From: Taf14 recognizes a common motif in transcriptional machineries and facilitates their clustering by phase separation

Fig. 2

a Two orthogonal views of the Taf14ET–Sth1EBM complex. Taf14ET is colored in green and Sth1EBM is colored in cyan. b The interface between Taf14ET and Sth1EBM. Sth1ET is shown as a surface model colored according to its electrostatic potential (positive potential: blue; negative potential, red). The residues through which Sth1EBM interacts with the Taf14ET are presented as ball-and-stick models. The four acidic residues of Taf14ET are labeled. c Details of hydrophobic interactions. The critical residues are presented as ball-and-stick models. d ITC results showing that the targeted mutations decreased the affinity of the interaction between Taf14ET and Sth1EBM. M4 stands for the Sth1L1204A/V1206A/I1208A/L1210A mutation. e Co-immunoprecipitation using an HA antibody showed that Sth1M4 mutation weakened the interaction with Taf14. Taf14 was tagged with HA; Sth1 was tagged with TAP. TCL total cell lysate, IP immune-precipitation, IB immune-blot. Source data are provided as a Source Data file.

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