Dynamic switch of the signal recognition particle from scanning to targeting.
Open accessAbstract
Ribosomes synthesizing inner membrane proteins in Escherichia coli are targeted to the membrane by the signal recognition particle (SRP) pathway. By rapid kinetic analysis we show that after initial binding to the ribosome, SRP undergoes dynamic fluctuations in search of additional interactions. Non-translating ribosomes, or ribosomes synthesizing non-membrane proteins, do not provide these contacts, allowing SRPs to dissociate rapidly. A nascent peptide in the exit tunnel stabilizes SRPs in a standby state. Binding to the emerging signal-anchor sequence (SAS) of a nascent membrane protein halts the fluctuations of SRP, resulting in complex stabilization and recruitment of the SRP receptor. We propose a kinetic model where SRP rapidly scans all ribosomes until it encounters a ribosome exposing an SAS. Binding to the SAS switches SRP into the targeting mode, in which dissociation is slow and docking of the SRP receptor is accelerated.
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SRP binds to vacant ribosomes with high affinity (Kd 50-60 nM).
“SRP binds to vacant ribosomes with high affinity (Kd 50–60 nM)”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Holtkamp et al., 2012
When the nascent chain reaches a length of approx. 45-50 amino acids and the signal anchor sequence is exposed to the outside of the ribosome, SRP forms a stable complex with the ribosome-associated nascent chain (RNC) (Kd ≤ 1 nM).
“When the nascent chain reaches a length of approx. 45–50 amino acids and the signal anchor sequence is exposed to the outside of the ribosome, SRP forms a stable complex with the ribosome-associated nascent chain (RNC) (Kd ≤ 1 nM)”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Holtkamp et al., 2012
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References 32 · Cited by 81
Research works printed but not linked: 1
- Published online at http://www.nature.com/doifinder/10.1038/nsmb.2421. Reprints and permissions information is available online at http://www.nature.com/ reprints/index.html.
- Authors
- Holtkamp, W., Lee, S., Bornemann, T., Senyushkina, T., Rodnina, M. V., & Wintermeyer, W.
- Affiliations
- Max Planck Institute for Biophysical Chemistry (DE)
- Corresponding author
- Wintermeyer, Wolfgang
- Venue
- Nature Structural & Molecular Biology
- Published
- 2012-11-11
- Volume
- 19
- Issue
- 12
- Pages
- 1332-1337
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2055687096
- Cited by
- 81
- References
- 32
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 2 · 2023: 2 · 2022: 3 · 2021: 8 · 2020: 2 · 2019: 6 · 2018: 4 · 2017: 7 · 2016: 6 · 2015: 13 · 2014: 16 · 2013: 8
- FWCI
- 4.75
- Type
- journal article
- Language
- en
- Open access
- green
- hdl.handle.net
- Licence
- other-oa
- www.springer.com/tdm (tdm)
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion, other-oa)
- GRO (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- 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 › Cell Biology › Cellular transport and secretion
- Keywords
- signal recognition particle, ribosome scanning, signal-anchor sequence, nascent polypeptide chains, SRP receptor, membrane protein targeting, kinetic model, Escherichia coli, protein-conducting channel
- MeSH terms
- Half-Life, Kinetics, Signal Recognition Particle
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