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. Author manuscript; available in PMC: 2010 Mar 24.
Published in final edited form as: Biochemistry. 2008 Jun 24;47(25):6719–6726. doi: 10.1021/bi800309m

Figure 1.

Figure 1

MST1 preparation and characterization. (A) The construct designs for the various protein fragments of MST1 used for this study are depicted. The various domains are abbreviated as follows: KD, kinase domain; RR, regulatory region; and DD, dimerization domain. (B) SDS page gel of the various recombinant protein constructs used in this study. The abbreviations are as follows: MST1-FL, full-length MST1; MST1-KD/RR, MST1 kinase with the regulatory region, spanning residues 1–380; and MST1-FL (TM), MST1-FL triple mutant with residues S340, T346, and T348 mutated to alanine. (C) Autoradiography gel showing the activity of MST1 toward phosphorylation of its substrates, FoxO1 and histone H2B. The signal depicted is the incorporation of the γ-32P label onto FoxO and histone H2B. The autophosphorylation signal of MST1 is also visible as indicated. (D) Autoradiograph showing the effect of DNA binding on the phosphorylation activity of FoxO1 by MST1-FL in the presence and absence of its cognate DNA, the Daf-16 binding element