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Architecture of chloroplast TOC–TIC translocon supercomplex

Author

Listed:
  • Hao Liu

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Anjie Li

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Jean-David Rochaix

    (University of Geneva
    University of Geneva)

  • Zhenfeng Liu

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

Abstract

Chloroplasts rely on the translocon complexes in the outer and inner envelope membranes (the TOC and TIC complexes, respectively) to import thousands of different nuclear-encoded proteins from the cytosol1–4. Although previous studies indicated that the TOC and TIC complexes may assemble into larger supercomplexes5–7, the overall architectures of the TOC–TIC supercomplexes and the mechanism of preprotein translocation are unclear. Here we report the cryo-electron microscopy structure of the TOC–TIC supercomplex from Chlamydomonas reinhardtii. The major subunits of the TOC complex (Toc75, Toc90 and Toc34) and TIC complex (Tic214, Tic20, Tic100 and Tic56), three chloroplast translocon-associated proteins (Ctap3, Ctap4 and Ctap5) and three newly identified small inner-membrane proteins (Simp1–3) 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. Four lipid molecules are located within or above an inner-membrane funnel formed by Tic214, Tic20, Simp1 and Ctap5. Multiple potential pathways found in the TOC–TIC supercomplex may support translocation of different substrate preproteins into chloroplasts.

Suggested Citation

  • Hao Liu & Anjie Li & Jean-David Rochaix & Zhenfeng Liu, 2023. "Architecture of chloroplast TOC–TIC translocon supercomplex," Nature, Nature, vol. 615(7951), pages 349-357, March.
  • Handle: RePEc:nat:nature:v:615:y:2023:i:7951:d:10.1038_s41586-023-05744-y
    DOI: 10.1038/s41586-023-05744-y
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    Cited by:

    1. Sarah E. Hanson & Tyrone Dowdy & Mioara Larion & Matthew Thomas Doyle & Harris D. Bernstein, 2024. "The patatin-like protein PlpD forms structurally dynamic homodimers in the Pseudomonas aeruginosa outer membrane," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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