Asymmetric binding of membrane proteins to GroEL. Academic Article

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.

authors

• Young, Ryland

published proceedings

• Arch Biochem Biophys

author list (cited authors)

• Sun, J., Savva, C. G., Deaton, J., Kaback, H. R., Svrakic, M., Young, R. y., & Holzenburg, A.

citation count

• 10

complete list of authors

• Sun, Jingchuan||Savva, Christos G||Deaton, John||Kaback, H Ronald||Svrakic, Maja||Young, Ry||Holzenburg, Andreas

publication date

• January 2005

publisher

• Elsevier  Publisher

published in

• Archives of Biochemistry and Biophysics  Journal

keywords

• Bacteriorhodopsins
• Biochemistry
• Cell Membrane
• Chaperonin 60
• Crystallography, X-Ray
• Image Processing, Computer-Assisted
• Imaging, Three-Dimensional
• Lipid Bilayers
• Membrane Transport Proteins
• Microscopy, Electron
• Models, Molecular
• Protein Binding
• Protein Conformation
• Viral Proteins

Digital Object Identifier (DOI)

• 10.1016/j.abb.2004.11.021

start page

• 352

end page

• 357

volume

• 434

issue

• 2

URL

• http://dx.doi.org/10.1016/j.abb.2004.11.021