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FIGURE 2. Yeast Rtn1p and Yop1p form homo-oligomers in the membrane. A, membranes isolated from wild-type or rtn1Δrtn2Δyop1Δ (NDY257) yeast cells expressing wild-type or mutant forms of Rtn1-GFP at endogenous levels were solubilized in 1% digitonin, fractionated by 5–30% w/v sucrose gradient centrifugation, and analyzed by SDS-PAGE and immunoblotting with anti-GFP antibody. Note that the mutant forms of Rtn1p have peak migrations at a smaller molecular weight than the wild-type protein. B, membranes isolated from wild-type or rtn1Δrtn2Δyop1Δ yeast cells expressing wild-type Yop1-GFP at endogenous levels were solubilized in 1% digitonin and were analyzed as in A. Molecular weight standards in the sucrose gradient are as indicated. C, isolated membranes of yeast cells expressing Rtn1-His were treated with increasing concentrations of EGS and analyzed on SDS-PAGE, and oligomers were visualized by immunoblotting with anti-His antibody. D, membranes of yeast cells expressing Yop1-HA were analyzed as in C and immunoblotted with anti-HA antibody. Asterisks, number of monomeric copies of the specified protein as seen by SDS-PAGE. Image published in: Shibata Y et al. (2008) Copyright © 2008, The American Society for Biochemistry and Molecular Biology, Inc. This image is reproduced with permission of the journal and the copyright holder. This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license Larger Image Printer Friendly View

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