The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Structure of the Mammalian Ribosome-Sec61 Complex to 3.4 Å Resolution
Open accessAbstract
Cotranslational protein translocation is a universally conserved process for secretory and membrane protein biosynthesis. Nascent polypeptides emerging from a translating ribosome are either transported across or inserted into the membrane via the ribosome-bound Sec61 channel. Here, we report structures of a mammalian ribosome-Sec61 complex in both idle and translating states, determined to 3.4 and 3.9 Å resolution. The data sets permit building of a near-complete atomic model of the mammalian ribosome, visualization of A/P and P/E hybrid-state tRNAs, and analysis of a nascent polypeptide in the exit tunnel. Unprecedented chemical detail is observed for both the ribosome-Sec61 interaction and the conformational state of Sec61 upon ribosome binding. Comparison of the maps from idle and translating complexes suggests how conformational changes to the Sec61 channel could facilitate translocation of a secreted polypeptide. The high-resolution structure of the mammalian ribosome-Sec61 complex provides a valuable reference for future functional and structural studies.
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Cites
RELION: Implementation of a Bayesian approach to cryo-EM structure determination
Scheres, S. H. W. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.09.006 · Cited by 5,446
Self-citationRosenthal, P. B., & Henderson, R. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.07.013 · Cited by 2,416
Structure of a complex of the ATPase SecA and the protein-translocation channel.
Zimmer, J., Nam, Y., & Rapoport, T. A. (2008) · Nature · doi:10.1038/nature07335 · Cited by 459
Structure of the SecY channel during initiation of protein translocation
Park, E., Ménétret, J.-F., Gumbart, J. C., Ludtke, S. J., Li, W., Whynot, A., Rapoport, T. A., & Akey, C. W. (2014) · Nature · doi:10.1038/nature12720 · Cited by 148
Ribosome binding of a single copy of the SecY complex: implications for protein translocation.
Ménétret, J.-F., Schaletzky, J., Clemons, W. M., Osborne, A. R., Skånland, S. S., Denison, C., Gygi, S. P., Kirkpatrick, D. S., Park, E., Ludtke, S. J., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.10.034 · Cited by 108
Cited by
Protein export through the bacterial Sec pathway
Tsirigotaki, A., De Geyter, J., Šoštaric´, N., Economou, A., & Karamanou, S. (2017) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2016.161 · Cited by 447
The mammalian ribo-interactome reveals ribosome functional diversity and heterogeneity
Simsek, D., Tiu, G. C., Flynn, R. A., Byeon, G. W., Leppek, K., Xu, A. F., Chang, H. Y., & Barna, M. (2017) · Cell · doi:10.1016/j.cell.2017.05.022 · Cited by 439
Local and global influences on protein turnover in neurons and glia
Dörrbaum, A. R., Kochen, L., Langer, J. D., & Schuman, E. M. (2018) · eLife · doi:10.7554/elife.34202 · Cited by 249
Root of the Tree: The Significance, Evolution, and Origins of the Ribosome
Bowman, J. C., Petrov, A. S., Frenkel-Pinter, M., Penev, P. I., & Williams, L. D. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00742 · Cited by 197
Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon
Jomaa, A., Boehringer, D., Leibundgut, M., & Ban, N. (2016) · Nature Communications · doi:10.1038/ncomms10471 · Cited by 115
Metadata
- Authors
- Voorhees, R. M., Fernández, I. S., Scheres, S. H. W., & Hegde, R. S.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2014-06
- Volume
- 157
- Issue
- 7
- Pages
- 1632-1643
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2064254630
- Cited by
- 339
- References
- 5
- FWCI
- 13.99
- Type
- journal article
- Language
- en
- Open access
- hybrid
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