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Structure of the E. coli signal recognition particle bound to a translating ribosome.
Open accessAbstract
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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Erratum: Structure of the E. coli signal recognition particle bound to a translating ribosome
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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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