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Structure of the E. coli signal recognition particle bound to a translating ribosome.
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The prokaryotic signal recognition particle (SRP) targets membrane proteins into the inner membrane. It binds translating ribosomes and screens the emerging nascent chain for a hydrophobic signal sequence, such as the transmembrane helix of inner membrane proteins. If such a sequence emerges, the SRP binds tightly, allowing the SRP receptor to lock on. This assembly delivers the ribosome-nascent chain complex to the protein translocation machinery in the membrane. Using cryo-electron microscopy and single-particle reconstruction, we obtained a 16 A structure of the Escherichia coli SRP in complex with a translating E. coli ribosome containing a nascent chain with a transmembrane helix anchor. We also obtained structural information on the SRP bound to an empty E. coli ribosome. The latter might share characteristics with a scanning SRP complex, whereas the former represents the next step: the targeting complex ready for receptor binding. High-resolution structures of the bacterial ribosome and of the bacterial SRP components are available, and their fitting explains our electron microscopic density. The structures reveal the regions that are involved in complex formation, provide insight into the conformation of the SRP on the ribosome and indicate the conformational changes that accompany high-affinity SRP binding to ribosome nascent chain complexes upon recognition of the signal sequence.
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“Substrate recognition by SRP is a multi-step process that is initiated by SRP binding to the ribosome, where it contacts primarily uL23, uL29, and the 23S rRNA close to the tunnel exit”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Schaffitzel et al., 2006
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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,723
Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,616
SPIDER and WEB: Processing and Visualization of Images in 3D Electron Microscopy and Related Fields
Frank, J., Radermacher, M., Penczek, P. A., Zhu, J., Li, Y., Ladjadj, M., & Leith, A. G. (1996) · Journal of Structural Biology · doi:10.1006/jsbi.1996.0030 · Cited by 2,026
Structures of the Bacterial Ribosome at 3.5 A Resolution
Schuwirth, B. S., Borovinskaya, M. A., Hau, C. W., Zhang, W., Vila‐Sanjurjo, A., Holton, J. M., & Cate, J. H. D. (2005) · Science · doi:10.1126/science.1117230 · Cited by 1,417
Walter, P., & Blobel, G. (1982) · Nature · doi:10.1038/299691a0 · Cited by 779
The Signal Recognition Particle
Keenan, R. J., Freymann, D. M., Stroud, R. M., & Walter, P. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.755 · Cited by 639
Situs: A Package for Docking Crystal Structures into Low-Resolution Maps from Electron Microscopy
Wriggers, W. R., Milligan, R. A., & McCammon, J. A. (1999) · Journal of Structural Biology · doi:10.1006/jsbi.1998.4080 · Cited by 521
Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
Ferbitz, L., Maier, T., Patzelt, H., Bukau, B., Deuerling, E., & Ban, N. (2004) · Nature · doi:10.1038/nature02899 · Cited by 419
Self-citationStructure of the signal recognition particle interacting with the elongation-arrested ribosome
Halić, M., Becker, T. A., Pool, M., Spahn, C. M. T., Grassucci, R. A., Frank, J., & Beckmann, R. (2004) · Nature · doi:10.1038/nature02342 · Cited by 418
Wyngaard, J. (1988) · American Meteorological Society eBooks · doi:10.1007/978-1-935704-16-4_2 · Cited by 414
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Driessen, A. J. M., & Nouwen, N. P. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.061606.160747 · Cited by 635
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Janda, C. Y., Li, J., Oubridge, C., Hernández, H., Robinson, C. V., & Nagai, K. (2010) · Nature · doi:10.1038/nature08870 · Cited by 197
Delivering proteins for export from the cytosol
Cross, B. C. S., Sinning, I., Luirink, J., & High, S. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2657 · Cited by 195
Kudva, R., Denks, K., Kuhn, P., Vogt, A., Müller, M., & Koch, H.-G. (2013) · Research in Microbiology · doi:10.1016/j.resmic.2013.03.016 · Cited by 177
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Denks, K., Vogt, A., Sachelaru, I., Petriman, N.-A., Kudva, R., & Koch, H.-G. (2014) · Molecular Membrane Biology · doi:10.3109/09687688.2014.907455 · Cited by 170
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Merz, F., Boehringer, D., Schaffitzel, C., Preißler, S., Hoffmann, A., Maier, T., Rutkowska, A., Lozza, J., Ban, N., Bukau, B., et al. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.89 · Cited by 170
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Cabrita, L. D., Cassaignau, A. M. E., Launay, H., Waudby, C. A., Włodarski, T., Camilloni, C., Karyadi, M., Robertson, A. L., Wang, X., Wentink, A. S., et al. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3182 · Cited by 166
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Manuell, A. L., Quispe, J. D., & Mayfield, S. P. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050209 · Cited by 91
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Soung, G. Y., Miller, J. L., Koç, H., & Koc, E. C. (2009) · Journal of Proteome Research · doi:10.1021/pr900042e · Cited by 47
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Noriega, T. R., Tsai, A., Elvekrog, M., Petrov, A. N., Neher, S. B., Chen, J., Bradshaw, N., Puglisi, J. D., & Walter, P. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.563239 · Cited by 46
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Self-citationSarmah, P., Shang, W., Origi, A., Licheva, M., Kraft, C., Ulbrich, M. H., Lichtenberg, E., Wilde, A., & Koch, H. (2022) · Cell Reports · doi:10.1016/j.celrep.2023.112140 · Cited by 22
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Self-citationKnoops, K., Schoehn, G., & Schaffitzel, C. (2011) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.119 · Cited by 21
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Metadata
- Authors
- Schaffitzel, C., Oswald, M., Berger, I., Ishikawa, T., Abrahams, J. P., Koerten, H. K., Koning, R. I., & Ban, N.
- Affiliations
- ETH Zurich (CH)
- Leiden University (NL)
- Leiden University Medical Center (NL)
- Corresponding author
- Ban, Nenad
- ORCID
- Venue
- Nature
- Published
- 2006-10-29
- Volume
- 444
- Issue
- 7118
- Pages
- 503-506
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2050154932
- Cited by
- 136
- References
- 31
- Citations by year
- 2026: 4 · 2025: 3 · 2024: 2 · 2022: 5 · 2021: 4 · 2020: 4 · 2019: 9 · 2018: 3 · 2017: 5 · 2016: 7 · 2015: 10 · 2014: 10 · 2013: 7 · 2012: 3
- FWCI
- 4.89
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Leiden Repository (Leiden University) (submittedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- edoc (University of Basel) (submittedVersion)
- Explore Bristol Research (submittedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion, other-oa)
- Funders
- National Science Foundation
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Keywords
- signal recognition particle, Escherichia coli, ribosome-nascent chain complex, transmembrane helices, signal sequence recognition, SRP receptor, protein translocation, ribosome conformational change, ribosome structure
- MeSH terms
- Base Sequence, Binding Sites, Escherichia coli, Membrane Proteins, Models, Molecular, Molecular Sequence Data, Ribosomes, RNA, RNA, Ribosomal, Protein Biosynthesis, Signal Recognition Particle
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