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. 2018 May 7;115(21):E4833–E4842. doi: 10.1073/pnas.1803564115

Fig. 3.

Fig. 3.

Suppressors of the cut1, cut2, and rad21 mutants in the head and coiled coil of cohesin. (A) Locations of the suppressors of the cut1, cut2, and rad21 mutants (magenta, suppressors of the cut1 and cut2 mutants; cyan, suppressors of rad21-K1) (SI Appendix, Table S1 A and B). I67, which is responsible for the rad21-K1 mutant, is also identified (boxed). (Inset) Steric clashes (double-headed arrows) caused by I67F mutation in Rad21. The I67 side chain appears in white stick, and that of Phe in ball-and-stick. (B) Details of the two ATP binding sites at the head interface. ATP and Mg2+ are shown with sticks and green spheres, respectively. In A and B, yellow, green, and orange are used for Psm1, Psm3, and Rad21, respectively. α-Helices (A–I for Psm1/3, AN–CC for Rad21) and β-strands (1–15 for Psm1/3, 1C–3C for Rad21) are marked. The suffix indicates the N- or C-terminal domain of Rad21. (C) Immunochemical detection of phosphorylation level of Rad21 (upper bands) using a polyclonal anti-Rad21 antibody.