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A High-content Imaging Workflow to Study Grb2 Signaling Complexes by Expression Cloning
Published on: October 30, 2012
Asymmetric binding of membrane proteins to GroEL
Jingchuan Sun1, Christos G Savva, John Deaton
1Microscopy and Imaging Center, Texas A&M University, College Station, TX 77843-2257, USA. holzen@mic.tamu.edu
Abstract:
The interaction of GroEL with non-native soluble proteins has been studied intensively and structure-function relationships have been established in considerable detail. Recently, we found that GroEL is also able to bind membrane proteins in the absence of detergents and deliver them to liposomes in a biologically active state. Here, we report that three well-studied membrane proteins (bacteriorhodopsin, LacY, and the bacteriophage lambda holin) bind asymmetrically to tetradecameric GroEL. Each of the membrane proteins was visualized in one of the center cavities of GroEL using single particle analysis.
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