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. 1999 Aug;10(8):2607–2618. doi: 10.1091/mbc.10.8.2607

Figure 8.

Figure 8

The ability of Mad2p to rescue mad2-1 correlates with its ability to bind Mad1p. Cells used in the experiments are strains of wild-type (WT), mad2-1, mad2-1 containing a full-length MAD2 gene (FL), or a MAD2 gene that lacks regions encoding the N-terminal 5 (−N5, RHC88), C-terminal 5 (−C5, RHC89), N-terminal 10 (−N10, RHC91), or C-terminal 10 (−C10, RHC93) amino acids. (A) Co-immunoprecipitation between Mad1p and various Mad2p molecules. Lysates or Mad2p immunoprecipitated from exponentially growing cells were immunoblotted for either Mad1p (upper panels) or Mad2p (lower panels). (B) Benomyl sensitivity of various strains. Cells were spotted onto either YPD plates (left panel) or YPD plates containing 7.5 μg/ml benomyl (right panel). Cells were diluted 10-fold from the corresponding spot on the left. (C) Phosphorylation of Mad1p in various strains. Cells were first arrested at early G1 with α-factor and then released from the arrest into YPD containing 30 μg/ml benomyl and 10 μg/ml nocodazole. Aliquots of cells were taken every 30 min as indicated. Cell lysates were prepared and immunoblotted for Mad1p (upper panel) or Clb2p (lower panel).