Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 434, Issue 2, Pages 352-357Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2004.11.021
Keywords
membrane proteins; GroEL; 3D structure solubilization; electron microscopy; single particle analysis; 3D reconstruction
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Funding
- NIGMS NIH HHS [R01 GM027099, GM27077] Funding Source: Medline
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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. (C) 2004 Elsevier Inc. All rights reserved.
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