SRP-dependent co-translational targeting and SecA-dependent translocation analyzed as individual steps in the export of a bacterial protein.
Open accessAbstract
Recently it has been recognized that the signal recognition particle (SRP) of Escherichia coli represents a specific targeting device for hydrophobic inner membrane proteins. It has remained unclear, however, whether the bacterial SRP functions in concert with SecA, which is required for the translocation of secretory proteins across the inner membrane. Here, we have analyzed a hybrid protein constructed by fusing the signal anchor sequence of an SRP-dependent inner membrane protein (MtlA) to the mature part of an exclusively SecA-requiring secretory protein (OmpA). We show that the signal anchor sequence of MtlA confers the novel properties onto nascent chains of OmpA of being co-translationally recognized and targeted to SecY by SRP. Once targeted to SecY, ribosome-associated nascent chains of the hybrid protein, however, remain untranslocated unless SecA is present. These results indicate that SRP and SecA cooperate in a sequential, non-overlapping manner in the topogenesis of those membrane proteins which, in addition to a signal anchor sequence, harbor a substantial hydrophilic domain to be translocated into the periplasm.
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Inner membrane proteins are targeted to the SecYEG translocon co-translationally as RNCs by the SRP pathway.
“Inner membrane proteins are targeted to the SecYEG translocon co-translationally as RNCs by the SRP pathway (Figure 2; Koch et al., 1999; Beck et al., 2000; Neumann-Haefelin et al., 2000; Akopian et al., 2013b; Steinberg et al., 2018).”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Neumann-Haefelin et al., 2000
A similar situation is encountered during co-translational insertion of membrane proteins with large periplasmic loops, because their translocation requires SecA.
“A similar situation is encountered during co-translational insertion of membrane proteins with large periplasmic loops, because their translocation requires SecA (Neumann-Haefelin et al., 2000; Deitermann et al., 2005).”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Neumann-Haefelin et al., 2000
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Self-citation
- Authors
- Neumann‐Haefelin, C., Schäfer, U., Müller, M., & Koch, H.
- Affiliations
- University of Freiburg (DE)
- Corresponding author
- Neumann‐Haefelin, Christoph
- Venue
- The EMBO Journal
- Published
- 2000-12-01
- Volume
- 19
- Issue
- 23
- Pages
- 6419-6426
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC305875
- OpenAlex
- W1970875996
- Cited by
- 135
- References
- 32
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 1 · 2023: 1 · 2022: 4 · 2021: 2 · 2020: 2 · 2019: 4 · 2018: 2 · 2017: 3 · 2016: 6 · 2015: 4 · 2014: 9 · 2013: 4 · 2012: 1
- FWCI
- 6.80
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- FreiDok plus (Universitätsbibliothek Freiburg) (submittedVersion)
- Funders
- European Commission
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- signal recognition particle, SecA, protein translocation, SecY, OmpA, hybrid proteins, signal-anchor sequence, periplasmic export, inner membrane proteins, Escherichia coli, hydrophobic membrane proteins
- MeSH terms
- SEC Translocation Channels, SecA Proteins, Adenosine Triphosphatases, Bacterial Outer Membrane Proteins, Bacterial Proteins, Carrier Proteins, Cell Membrane, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Proton-Translocating ATPases, Models, Biological, Monosaccharide Transport Proteins, Mutation, Phosphoenolpyruvate Sugar Phosphotransferase System, Plasmids, Recombinant Fusion Proteins, Ribosomes, Protein Biosynthesis, Signal Recognition Particle, Peptidylprolyl Isomerase, Periplasm, Protein Transport, Membrane Transport Proteins, Escherichia coli Proteins
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