Phospholipids are needed for the proper formation, stability, and function of the photoactivated rhodopsin-transducin complex.

ABSTRACT: Heterotrimeric G proteins become activated after they form a catalytically active complex with activated G protein-coupled receptors (GPCRs) and GTP replaces GDP on the G protein alpha-subunit. This transient coupling can be stabilized by nucleotide depletion, resulting in an empty-nucleotide G protein-GPCR complex. Efficient and reproducible formation of conformationally homogeneous GPCR-Gt complexes is a prerequisite for structural studies. Herein, we report isolation conditions that enhance the stability and preserve the activity and proper stoichiometry of productive complexes between the purified prototypical GPCR, rhodopsin (Rho), and the rod cell-specific G protein, transducin (Gt). Binding of purified Gt to photoactivated Rho (Rho*) in n-dodecyl beta-D-maltoside (DDM) examined by g

SUBMITTER: Jastrzebska B 

PROVIDER: S-EPMC2753473 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature