The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Structure of the mitochondrial import gate reveals distinct preprotein paths
Open accessAbstract
The translocase of the outer mitochondrial membrane (TOM) is the main entry gate for proteins1–4. Here we use cryo-electron microscopy to report the structure of the yeast TOM core complex5–9 at 3.8-Å resolution. The structure reveals the high-resolution architecture of the translocator consisting of two Tom40 β-barrel channels and α-helical transmembrane subunits, providing insight into critical features that are conserved in all eukaryotes1–3. Each Tom40 β-barrel is surrounded by small TOM subunits, and tethered by two Tom22 subunits and one phospholipid. The N-terminal extension of Tom40 forms a helix inside the channel; mutational analysis reveals its dual role in early and late steps in the biogenesis of intermembrane-space proteins in cooperation with Tom5. Each Tom40 channel possesses two precursor exit sites. Tom22, Tom40 and Tom7 guide presequence-containing preproteins to the exit in the middle of the dimer, whereas Tom5 and the Tom40 N extension guide preproteins lacking a presequence to the exit at the periphery of the dimer. The high-resolution cryo-electron microscopy structure of the yeast translocase of the outer mitochondrial membrane reveals key features of mitochondrial protein import that are conserved in all eukaryotes.
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Cites
MAFFT Multiple Sequence Alignment Software Version 7: Improvements in Performance and Usability
Katoh, K., & Standley, D. M. (2013) · Molecular Biology and Evolution · doi:10.1093/molbev/mst010 · Cited by 46,209
PHENIX : a comprehensive Python-based system for macromolecular structure solution
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Mitochondrial proteins: from biogenesis to functional networks
Pfanner, N., Warscheid, B., & Wiedemann, N. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0092-0 · Cited by 1,028
Self-citationA Disulfide Relay System in the Intermembrane Space of Mitochondria that Mediates Protein Import
Mesecke, N., Terziyska, N., Kozany, C., Baumann, F., Neupert, W., Hell, K., & Herrmann, J. M. (2005) · Cell · doi:10.1016/j.cell.2005.04.011 · Cited by 557
Bien, M., Longen, S., Wagener, N., Chwalla, I., Herrmann, J. M., & Riemer, J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.017 · Cited by 179
Cited by
Spatial arrangement of proteins in planar and curved membranes by PPM 3.0
Lomize, A. L., Todd, S. C., & Pogozheva, I. D. (2022) · Protein Science · doi:10.1002/pro.4219 · Cited by 339
Molecular pathway of mitochondrial preprotein import through the TOM–TIM23 supercomplex
Zhou, X., Yang, Y., Wang, G., Wang, S., Sun, D., Ou, X., Lian, Y., & Li, L. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01103-7 · Cited by 72
Mechanism of human PINK1 activation at the TOM complex in a reconstituted system
(2024) · doi:10.1126/sciadv.adn7191 · Cited by 39
Muthukumar, G., Stevens, T. A., Inglis, A. J., Esantsi, T. K., Saunders, R. A., Schulte, F., Voorhees, R. M., Guna, A., & Weissman, J. S. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.01.028 · Cited by 34
Two conformations of the Tom20 preprotein receptor in the TOM holo complex
Ornelas, P., Bausewein, T., Martin, J., Morgner, N., Nussberger, S., & Kühlbrandt, W. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2301447120 · Cited by 27
Metadata
- Authors
- Araiso, Y., Tsutsumi, A., Qiu, J., Imai, K., Shiota, T., Song, J., Lindau, C., Wenz, L.-S., Sakaue, H., Yunoki, K., Kawano, S., Suzuki, J., Wischnewski, M., Schütze, C., Ariyama, H., Ando, T., Becker, T., Lithgow, T., Wiedemann, N., Pfanner, N., Kikkawa, M., & Endo, T.
- Venue
- Nature
- Published
- 2019-10-10
- Volume
- 575
- Issue
- 7782
- Pages
- 395-401
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2979472203
- Cited by
- 246
- References
- 5
- FWCI
- 7.45
- Type
- journal article
- Language
- en
- Open access
- green
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- Araiso, Y., Tsutsumi, A., Qiu, J., Imai, K., Shiota, T., Song, J., Lindau, C., Wenz, L.-S., Sakaue, H., Yunoki, K., Kawano, S., Suzuki, J., Wischnewski, M., Schütze, C., Ariyama, H., Ando, T., Becker, T., Lithgow, T., Wiedemann, N., . . . Endo, T. (2019). Structure of the mitochondrial import gate reveals distinct preprotein paths. Nature. https://doi.org/10.1038/s41586-019-1680-7
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