Skip to main content
. 2003 Aug 15;17(16):1957–1962. doi: 10.1101/gad.1099003

Figure 1.

Figure 1.

Effect of the C-terminal deletion of Xrs2 on DNA sensitivity and the complex formation. (A,B) Sensitivity to phleomycin (A) and UV light (B). Serial dilutions of cultures were spotted on YEPD media without or with phleomycin. Cultures spotted on YEPD media were irradiated with UV light. All of the strains contain the sml1Δ mutation that suppresses the lethality of mec1 mutants (Zhao et al. 1998). Strains used were wild-type (KSC1560), xrs2Δ (KSC1562), xrs2-11 (KSC1563), tel1Δ (KSC1661), mec1-81 (KSC1662), mec1-81 tel1Δ (KSC1564), mec1-81 xrs2-11 (KSC1565), and mec1-81 tel1Δ xrs2-11 (KSC1566). (C) Interaction between Tel1and Xrs2. Cells were untreated (–) or treated with 50 μg/mL phleomycin for 1h (+). Extracts were prepared from cells and immunoprecipitated with anti-HA antibodies. Immunoprecipitates (IP) and whole extracts were subjected to immunoblotting analysis. Strains used were XRS2-myc (KSC1904), xrs2-11-myc (KSC1905), TEL1-HA (KSC1785), TEL1-HA XRS2-myc (KSC1906), and TEL1-HA xrs2-11-myc (KSC1907). (D) Interaction of Xrs2 with Mre11 and Rad50. Extracts were prepared from XRS2-HA (KSC1744), xrs2-11-HA (KSC1869), or untagged cells (KSC1516), and immunoprecipitated with anti-HA antibodies. IPs and whole extracts were subjected to immunoblotting analysis. Phosphatase treatment diminished the slower migrating forms of Xrs2-HA and Xrs2-11-HA (data not shown), suggesting that Xrs2 and Xrs2-11 are phosphorylated proteins.