Xenbase Image ID: 125852

FIGURE 6. Xenopus CMG complex. Chromatin was isolated from egg extract in the middle of S-phase (when replisome proteins peak on chromatin), and proteins were released from chromatin in presence of 50, 100, or 300 mm potassium acetate. A, soluble chromatin protein complexes were separated by gel filtration and glycerol gradient and CMG components (Mcm2-7, Cdc45, and GINS) were followed through fractionation by immunoblotting. The data were used (19) to determine the molecular weight of the complexes. B and C, mid-S phase chromatin solubilized in 300 mm potassium acetate was immunoprecipitated with non-immune or anti-Cdc45 antibodies. Proteins present in the immunoprecipitates were analyzed by immunoblotting (B) or by mass spectrometry (C). Image published in: Gambus A et al. (2011) © 2011 by The American Society for Biochemistry and Molecular Biology, Inc. Creative Commons Attribution-NonCommercial license Larger Image Printer Friendly View

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