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. 2001 Nov 26;155(5):763–774. doi: 10.1083/jcb.200105029

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Copyright © 2001, The Rockefeller University Press

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Figure 3. — Ipl1 phosphorylates Sli15 and is activated by Sli15. (A) In vitro phosphorylation of Sli15 by Ipl1 and [γ-³²P]ATP. With the exception of bovine MBP, all proteins used were purified from E. coli. The asterisks denote labeled GST–Ipl1 bands caused by autophosphorylation. (B) Stimulation of GST–Ipl1 kinase activity by GST–Sli15-C. MBP (1 μg) was phosphorylated by GST–Ipl1 (0.6 μg) in the presence of various amounts of GST–Sli15-C. (C) Phosphorylation of Sli15 is altered in ipl1 mutant cells. Wild-type (WT) (CCY766-9D) or ipl1-2 (CCY915-13C) cells carrying pCC1301 (Sli15–HA) were incubated in supplemented synthetic complete (SC) medium lacking leucine at 26°C and then shifted to 37°C for 2.5 h. Protein extracts from these cells were analyzed by immunoblotting with anti-HA or anti-G6PDH antibodies.

Figure 3. — Ipl1 phosphorylates Sli15 and is activated by Sli15. (A) In vitro phosphorylation of Sli15 by Ipl1 and [γ-³²P]ATP. With the exception of bovine MBP, all proteins used were purified from E. coli. The asterisks denote labeled GST–Ipl1 bands caused by autophosphorylation. (B) Stimulation of GST–Ipl1 kinase activity by GST–Sli15-C. MBP (1 μg) was phosphorylated by GST–Ipl1 (0.6 μg) in the presence of various amounts of GST–Sli15-C. (C) Phosphorylation of Sli15 is altered in ipl1 mutant cells. Wild-type (WT) (CCY766-9D) or ipl1-2 (CCY915-13C) cells carrying pCC1301 (Sli15–HA) were incubated in supplemented synthetic complete (SC) medium lacking leucine at 26°C and then shifted to 37°C for 2.5 h. Protein extracts from these cells were analyzed by immunoblotting with anti-HA or anti-G6PDH antibodies.