Figure 5. Oligomerization facilitates... | Rockefeller University Press

Figure 5.

$Figure 5. Oligomerization facilitates the partitioning of TGBp3 to the cell periphery. (A) Yeast cells (SEY6210) expressing the proteins indicated were lysed, and the lysate (input) was subjected to pull-down by IgG Sepharose. Samples were analyzed by anti-GFP and anti-PA immunoblots. (B) Yeast cells (SEY6210) expressing various GFP-TGBp3 mutants were size-fractionated on a Superose 6 column. Fractions were analyzed by immunoblotting with anti-GFP antibody (left), and the results were quantified and plotted (right). The elution of molecular weight standards is indicated. (C) Same as B except that a nontagged TGBp3 was overexpressed in cells expressing I33A or G44A GFP-TGBp3. (C, bottom) The plots compare the fractionation profiles for I33A and G44A GFP-TGBp3 in B and C. (D) Various GFP-TGBp3 mutants were transformed with empty vector (−) or a vector overexpressing nontagged TGBp3 (+). The cells were imaged by confocal microscopy (top) and quantified (bottom). Bar, 5 µm.$

Oligomerization facilitates the partitioning of TGBp3 to the cell periphery. (A) Yeast cells (SEY6210) expressing the proteins indicated were lysed, and the lysate (input) was subjected to pull-down by IgG Sepharose. Samples were analyzed by anti-GFP and anti-PA immunoblots. (B) Yeast cells (SEY6210) expressing various GFP-TGBp3 mutants were size-fractionated on a Superose 6 column. Fractions were analyzed by immunoblotting with anti-GFP antibody (left), and the results were quantified and plotted (right). The elution of molecular weight standards is indicated. (C) Same as B except that a nontagged TGBp3 was overexpressed in cells expressing I33A or G44A GFP-TGBp3. (C, bottom) The plots compare the fractionation profiles for I33A and G44A GFP-TGBp3 in B and C. (D) Various GFP-TGBp3 mutants were transformed with empty vector (−) or a vector overexpressing nontagged TGBp3 (+). The cells were imaged by confocal microscopy (top) and quantified (bottom). Bar, 5 µm.