Asymmetric binding of membrane proteins to GroEL.
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.
Sun
Jingchuan
J
Microscopy and Imaging Center, Texas A&M University, College Station, TX 77843-2257, USA. holzen@mic.tamu.edu
Savva
Christos G
CG
Deaton
John
J
Kaback
H Ronald
HR
Svrakic
Maja
M
Young
Ry
R
Holzenburg
Andreas
A
D001436:Bacteriorhodopsins / Q000737:chemistry; D001671:Biochemistry / Q000379:methods*; D002462:Cell Membrane / Q000378:metabolism; D018834:Chaperonin 60 / Q000378:metabolism / Q000502:physiology*; D018360:Crystallography, X-Ray; D007091:Image Processing, Computer-Assisted; D021621:Imaging, Three-Dimensional; D008051:Lipid Bilayers / Q000378:metabolism; D026901:Membrane Transport Proteins / Q000737:chemistry; D008854:Microscopy, Electron; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D014764:Viral Proteins / Q000737:chemistry
D018834:Chaperonin 60; D008051:Lipid Bilayers; D026901:Membrane Transport Proteins; C108624:S holin, bacteriophage lambda; D014764:Viral Proteins; D001436:Bacteriorhodopsins; C021499:lactose permease