Nature research paper: Architecture of chloroplast TOC-TIC translocon supercomplex
Chloroplasts rely on the translocon complexes in the outer and inner envelope membranes to import thousands of different nuclear-encoded proteins from the cytosol. While previous studies indicated that the TOC and TIC complexes may assemble into larger supercomplexes, the overall architectures of the TOC-TIC supercomplexes and the mechanism of preprotein translocation are elusive.
Here we report the cryo-electron microscopy structure of the TOC-TIC supercomplex fromat an overall resolution of 2.8 Å. The major subunits of the TOC complex and TIC complex , three chloroplast translocon-associated proteins and three newly-identified small inner-membrane proteins have been located in the supercomplex. As the largest protein, Tic214 traverses the inner membrane, the intermembrane space and the outer membrane, connecting the TOC complex with the TIC proteins. An inositol hexaphosphate molecule is located at the Tic214-Toc90 interface and stabilizes their assembly. Moreover, four lipid molecules are located within or above an inner-membrane funnel formed by Tic214, Tic20, Simp1 and Ctap5. Furthermore, multiple potential pathways found in the TOC-TIC supercomplex may support translocation of different substrate preproteins into chloroplasts.
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