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. 2003 Aug;14(8):3280–3291. doi: 10.1091/mbc.E03-03-0154

Figure 1.

Figure 1.

Role of Hsl1p and Hsl7p catalytic activities in Swe1p regulation. (A) Myc-tagged wild-type or K110R mutant Hsl1p proteins immunoprecipitated from yeast lysates (strains JMY1500 and DLY4640) were incubated together with [γ-32P]ATP to assess Hsl1p autophosphorylation (top) or immunoblotted to assess protein abundance (bottom). (B) The GAL1p-MIH1 strains JMY1340 (HSL1), JMY1289 (hsl1Δ), and DLY4994 (hsl1K110R) were grown on galactose-containing medium and cells were streaked out onto dextrose-containing medium to repress Mih1p expression. Microcolonies were photographed after 2 d at 30°C. (C) GST-tagged wild-type or G386A mutant Hsl7p proteins purified using glutathione-Sepharose were incubated together with [3H]S-adenosylmethionine and histone H2A to assess histone methylation (top) or stained with Coomassie Blue to assess protein abundance (middle, histone H2A; bottom, GST-Hsl7p). (D) The GAL1p-MIH1 strain JMY1290 (hsl7Δ) was transformed with plasmids containing HSL7 (pDLB1545), empty vector (YCplac111), or HSL7G386A (pDLB1608) and microcolonies were analyzed as described above.