Two homologous GTP-bindin proteins, atToc33 and atToc159, control access of cytosolic precursor proteins to the chloroplast, at Toc33 is a constitutive outer chloroplast membrane protein, whereas the precusor receptor atToc159 may be able to switch between a soluble and an integral membrane form. By transient expression of GFP fusion proteins, mutant analysis, and biochemical experimentation, we demonstrate that the GTP-binding domain regulates the targeting of cytosolic atToc159 to the chloroplast and mediates the switch between cytosolic and integral membrane forms. Mutant atToc159, unable to bind GTP, does not reinstate a green phenotype in an albino mutant (ppi2) lacking endogenous atToc159, remaining trapped in the cytosol. Thus, the function of atToc159 in chloroplast biogenesis is dependent on an intrinsic GTP-regulated swtich that controls localization of the receptor to the chloroplast envelope.
Bauer, Jörg; Hiltbrunner, Andreas; Weibel, Petra; Vidi, Pierre-Alexandre; Alvarez-Huerta, Mayte; Smith, Matthew D.; Schnell, Danny J.; and Kessler, Felix, "Essential Role of the G-Domain in Targeting of the Protein Import Receptor atToc159 to the Chloroplast Outer Membrane" (2002). Biology Faculty Publications. Paper 48.