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. 2001 Dec;12(12):3744–3758. doi: 10.1091/mbc.12.12.3744

Figure 3.

Figure 3

PCNA-like N-terminal domain of Rad9 interacts with Hus1 and Rad1. (A) Rad9, Rad9-N, and Rad9-C protein expression. Western blot of Rad9 immunoprecipitates, probed with anti-Rad9 antibody, from rad9Δ cells expressing pREP1 plasmid (pTE102, lane 1), pREP1-rad9+ (pTE479, lane 2), pREP1-rad9-N (pTE883, lane 3), and pREP1-rad9-C (pTE884, lane 4). A weaker signal in the same position as Rad9 in lanes 1, 3, and 4 is probably due to IgG heavy chain background. Lower molecular weight bands in lane 2 are likely the degradation products of Rad9. (B) Western blots of anti-Rad1 immunoprecipitations probed with anti-Hus1 (top) or anti-Rad1 antibody (bottom) from cells transformed with the same plasmids as in A. (C) Western blots of anti-Hus1 immunoprecipitations probed with anti-Hus1 (top) or anti-Rad1 antibody (bottom) from the same strains as used in A.