FIGURE 1.

XRCC1 interacts with ROS1 and ZDP. A and C, purified full-length ROS1 or truncated ROS1 polypeptides fused to a His tag were fixed to a nickel-Sepharose column. The proteins bound to the column were incubated in the presence of either MBP-XRCC1 or MBP alone. After washes, the proteins associated to the resin were separated by SDS-PAGE, transferred to a membrane, and immunoblotted with antibodies against MBP. B, MBP either alone or fused to XRCC1 (MBP-XRCC1) was expressed in E. coli and fixed to an amylose resin. His-tagged ROS1 purified from E. coli (His-ROS1) was incubated with either MBP-XRCC1 or MBP bound to the resin. After washes, the proteins associated to the resin were separated by SDS-PAGE, transferred to a membrane, and immunoblotted with antibodies against His₆ tag. D, schematic diagrams of full-length ROS1 and the different truncated ROS1 derivatives used in C: lysine-rich domain (yellow), DNA glycosylase domain (blue), and C-terminal domain (cyan). E, purified ZDP fused to His₆ tag was fixed to a nickel-Sepharose column and incubated in the presence of either MBP-XRCC1 or MBP alone. After washes, the proteins associated to the resin were separated by SDS-PAGE, transferred to a membrane, and immunoblotted with antibodies against MBP.