Toc34 is a preprotein receptor regulated by GTP and phosphorylation.

Most proteins present in chloroplasts are synthesized in the cytosol and are posttranslationally translocated into the organelle. A multicomponent translocation machinery located in both the outer and the inner envelope of chloroplasts was identified, but the mode of action of many subunits remains unclear. Here, we describe the regulation of an early step of translocation occurring at the outer envelope. The outer envelope translocon subunit Toc34 can be phosphorylated, and GTP binding is regulated by phosphorylation. In vitro, Toc34 acts as a receptor for proteins containing a chloroplast-targeting signal. Interaction of Toc34 with the transit peptide is highly regulated and depends on GTP binding to Toc34 and on phosphorylation of the transit peptide of the preprotein.