Figure 4. L³⁸⁵ and F³⁸⁹ are critical for Rad21 to interact with SA2.

(A) Sequence alignment of Rad21 from various vertebrate species. The sequence alignment was prepared using BioEdit (http://www.mbio.ncsu.edu/bioedit/). The conserved Rad21 L³⁸⁵, F³⁸⁹ and T³⁹⁰ residues were used for making site-directed mutations. (B) Co-immunoprecipitation analysis indicating the importance of L³⁸⁵, F³⁸⁹, and T³⁹⁰ residues on Rad21 for its interaction with SA2. Flag-Rad21 and Myc-SA2(1–1051 aa) were expressed in 293 T cells. Co-IP was performed 48 h after transfection.