Cited by 189Bacterial Genetics and BiotechnologyRNA and protein synthesis mechanismsHeat shock proteins research

Discrimination between SRP- and SecA/SecB-dependent substrates involves selective recognition of nascent chains by SRP and trigger factor.

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Beck, Konstanze, Wu, Long‐Fei, Brunner, Josef, Müller, Matthias·2000·The EMBO Journal

Abstract

Besides SecA and SecB, Escherichia coli cells possess a signal recognition particle (SRP) to target exported proteins to the SecY translocon. Using chemical and site-specific cross-linking in vitro, we show that SRP recognizes the first signal anchor sequence of a polytopic membrane protein (MtlA) resulting in cotranslational targeting of MtlA to SecY and phospholipids of the plasma membrane. In contrast, a possible interaction of SRP with the secretory protein pOmpA is prevented by the association of trigger factor with nascent pOmpA. Trigger factor also prevents SecA from binding to the first 125 amino acids of pOmpA when they are still associated with the ribosome. Under no experimental conditions was SecA found to interact with MtlA. Likewise, virtually no binding of trigger factor to ribosome-bound MtlA occurs even in the complete absence of SRP. Collectively, our results indicate that at the stage of nascent polypeptides, polytopic membrane proteins are selected by SRP for co-translational membrane targeting, whereas secretory proteins are directed into the SecA/SecB-mediated post-translational targeting pathway by means of their preferential recognition by trigger factor.

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Crossref · 10.1093/emboj/19.1.134

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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 Beck et al., 2000

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Authors
Beck, K., Wu, L., Brunner, J., & Müller, M.
Affiliations
  • University of Freiburg (DE)
  • Centre National de la Recherche Scientifique (FR)
  • ETH Zurich (CH)
Corresponding author
Müller, Matthias
Venue
The EMBO Journal
Published
2000-01-04
Volume
19
Issue
1
Pages
134-143
ISSN
  • 0261-4189 (ISSN-L)
  • 1460-2075
OpenAlex
W2064351381
Cited by
189
References
47
Citations by year
2025: 6 · 2024: 1 · 2023: 4 · 2021: 2 · 2020: 1 · 2019: 7 · 2018: 4 · 2017: 2 · 2016: 3 · 2015: 3 · 2014: 7 · 2013: 7 · 2012: 6
FWCI
12.68
Type
journal article
Language
en
Open access
Locations
  • The EMBO Journal (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • FreiDok plus (Universitätsbibliothek Freiburg) (submittedVersion)
Funders
  • National Science Foundation
  • Deutscher Akademischer Austauschdienst
  • Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
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, precipitating factors, SecA, SecB, nascent polypeptide chains, signal-anchor sequence, polytopic membrane proteins, secreted proteins, Escherichia coli
MeSH terms
SEC Translocation Channels, SecA Proteins, Adenosine Triphosphatases, Bacterial Outer Membrane Proteins, Bacterial Proteins, Carrier Proteins, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Molecular Weight, Monosaccharide Transport Proteins, Phosphoenolpyruvate Sugar Phosphotransferase System, Protein Biosynthesis, Signal Recognition Particle, Peptidylprolyl Isomerase, Membrane Transport Proteins, Escherichia coli Proteins

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