Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • NEWS AND VIEWS

Path unveiled for protein entry into chloroplasts

Structures of the machinery for importing proteins into chloroplast organelles of algae, determined using cryo-electron microscopy, have opened a new chapter in efforts to understand how chloroplasts are built.
  1. Takashi Hirashima

    1. Takashi Hirashima is in the Faculty of Life Sciences and at the Institute for Protein Dynamics, Kyoto Sangyo University, Kyoto 603-8555, Japan.

    View author publications

    You can also search for this author in PubMed  Google Scholar

  2. Toshiya Endo

    1. Toshiya Endo is in the Faculty of Life Sciences and at the Institute for Protein Dynamics, Kyoto Sangyo University, Kyoto 603-8555, Japan.

    View author publications

    You can also search for this author in PubMed  Google Scholar

Chloroplasts are organelles, found in plants and algae, that house hundreds of different proteins responsible for photosynthesis, a process essential for life on Earth. Most chloroplast proteins are encoded by the nuclear genome, are made in the cytosol and contain a chloroplast-targeting signal. To be imported into the chloroplast, such proteins must cross the outer and inner envelope membranes (OEM and IEM, respectively) that surround the organelle. Protein complexes on the OEM (called TOC) and IEM (called TIC) form the intricate machinery that mediates protein transport across the two membranes1–3. Writing in Nature, Liu et al.4 report the cryo-electron microscopy (cryo-EM) structures of the TOC–TIC supercomplex from the unicellular green alga Chlamydomonas reinhardtii. This and another such structure reported in Cell by Jin et al.5 are the first high-resolution structures of the TOC and TIC complexes — they provide surprises and insights, but also raise many questions.

Access options

Rent or buy this article

Get just this article for as long as you need it

$39.95

Learn more

Prices may be subject to local taxes which are calculated during checkout

Nature 615, 222-224 (2023)

doi: https://doi.org/10.1038/d41586-023-00539-7

References

  1. Schleiff, E. & Becker, T. Nature Rev. Mol. Cell Biol. 12, 48–59 (2011).

    Article  PubMed  Google Scholar 

  2. Jarvis, P. & López-Juez, E. Nature Rev. Mol. Cell Biol. 14, 787–802 (2013).

    Article  PubMed  Google Scholar 

  3. Nakai, M. Biochim. Biophys. Acta Bioenerg. 1847, 957–967 (2015).

    Article  Google Scholar 

  4. Liu, H., Li, A., Rochaix, J.-D. & Liu, Z. Nature 615, 349–357 (2023).

    Article  Google Scholar 

  5. Jin, Z. et al. Cell 185, 4788–4800 (2022).

    Article  PubMed  Google Scholar 

  6. Ganesan, I., Shi, L.-X, Labs, M. & Theg, S. M. Plant Cell 30, 2161–2173 (2018).

    Article  PubMed  Google Scholar 

  7. Kikuchi, S. et al. Plant Cell 30, 2677–2703 (2018),

    Article  PubMed  Google Scholar 

  8. Chen, Y.-L. et al. Nature 564, 125–129 (2018).

    Article  PubMed  Google Scholar 

  9. Ramundo, S. et al. Proc. Natl Acad. Sci. USA 117, 32739–32749 (2020).

    Article  PubMed  Google Scholar 

Download references

Competing Interests

The authors declare no competing interests.

Subjects

Latest on:

Nature Careers

Jobs

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing

Search

Advanced search

Quick links