Cited by 76Bacterial Genetics and BiotechnologyRNA and protein synthesis mechanismsCellular transport and secretion

The bacterial SRP receptor, SecA and the ribosome use overlapping binding sites on the SecY translocon.

Open access
Kuhn, Patrick, Weiche, Benjamin, Sturm, Lukas, Sommer, Erik, Drepper, Friedel, Warscheid, Bettina, Sourjik, Victor, Koch, Hans‐Georg·2011·Traffic

Abstract

Signal recognition particle (SRP)‐dependent protein targeting is a universally conserved process that delivers proteins to the bacterial cytoplasmic membrane or to the endoplasmic reticulum membrane in eukaryotes. Crucial during targeting is the transfer of the ribosome‐nascent chain complex (RNC) from SRP to the Sec translocon. In eukaryotes, this step is co‐ordinated by the SRβ subunit of the SRP receptor (SR), which probably senses a vacant translocon by direct interaction with the translocon. Bacteria lack the SRβ subunit and how they co‐ordinate RNC transfer is unknown. By site‐directed cross‐linking and fluorescence resonance energy transfer (FRET) analyses, we show that FtsY, the bacterial SRα homologue, binds to the exposed C4/C5 loops of SecY, the central component of the bacterial Sec translocon. The same loops serve also as binding sites for SecA and the ribosome. The FtsY–SecY interaction involves at least the A domain of FtsY, which attributes an important function to this so far ill‐defined domain. Binding of FtsY to SecY residues, which are also used by SecA and the ribosome, probably allows FtsY to sense an available translocon and to align the incoming SRP–RNC with the protein conducting channel. Thus, the Escherichia coli FtsY encompasses the functions of both the eukaryotic SRα and SRβ subunits in one single protein.

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Crossref · 10.1111/j.1600-0854.2011.01167.x

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  • A simultaneous binding of SecA and the ribosome to SecY appears unlikely, considering that both engage overlapping binding sites on SecY.

    “A simultaneous binding of SecA and the ribosome to SecY appears unlikely, considering that both engage overlapping binding sites on SecY (Kuhn et al., 2011).”

    From The Dynamic SecYEG Translocon (2021) · cites this paper as Kuhn et al., 2011

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Research works printed but not linked: 6

  1. Halic M, Gartmann M, Schlenker O, Mielke T, Pool M, Sinning I, Beckmann R. The SRP receptor exposes the ribosomal translocon binding site. Science 2006;312:745-747.
  2. B ürk J, Weiche B, Wenk M, Boy D, Nestel S, Heimrich B, Koch HG. Depletion of the SRP receptor inactivates ribosomes in E. coli. J Bacteriol 2009;191:7017-7026.
  3. Parlitz R, Eitan A, Stjepanovic G, Bahari L, Bange G, Bibi E, Sinning I. E. coli SRP receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix. J Biol Chem 2007;282: 32176-32184.
  4. Mircheva M, Boy D, Weiche B, Hucke F, Graumann P, Koch HG. Predominant membrane localization is an essential feature of the bacterial SRP receptor. BMC Biol 2009;7:76.
  5. Angelini S, Deitermann S, Koch HG. FtsY, the bacterial SRP receptor interacts functionally and physically with the SecYEG translocon. EMBO Rep 2005;6:476-481.
  6. Park SK, Jiang F, Dalbey RE, Phillips GJ. Functional analysis of the signal recognition particle in Escherichia coli by characterization of a temperature-sensitive ffh mutant. J Bacteriol 2002;184:2642-2653.

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Authors
Kuhn, P., Weiche, B., Sturm, L., Sommer, E., Drepper, F., Warscheid, B., Sourjik, V., & Koch, H.
Affiliations
  • University of Freiburg (DE)
  • Heidelberg University (DE)
Corresponding author
Koch, Hans‐Georg
Venue
Traffic
Publisher
Wiley
Published
2011-02-25
Volume
12
Issue
5
Pages
563-578
ISSN
  • 1398-9219 (ISSN-L)
  • 1600-0854
OpenAlex
W2088921362
Cited by
76
References
75
Citations by year
2026: 1 · 2025: 2 · 2024: 1 · 2023: 1 · 2022: 2 · 2021: 4 · 2020: 4 · 2019: 6 · 2018: 7 · 2017: 6 · 2016: 6 · 2015: 8 · 2014: 8 · 2013: 9 · 2012: 3
FWCI
5.59
Type
journal article
Language
en
Open access
Locations
  • Traffic (publishedVersion)
  • PubMed (publishedVersion)
Funders
Deutsche Forschungsgemeinschaft (FOR 967, (EXC 294))
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 › Cell Biology › Cellular transport and secretion
Keywords
signal recognition particle, SRP receptor, FtsY, SecA, ribosome-nascent chain complex, protein translocation, Escherichia coli
MeSH terms
SEC Translocation Channels, SecA Proteins, Adenosine Triphosphatases, Bacterial Proteins, Binding Sites, Escherichia coli, Humans, Models, Molecular, Protein Binding, Ribosomes, Mass Spectrometry, Protein Structure, Tertiary, Receptors, Peptide, Receptors, Cytoplasmic and Nuclear, Signal Recognition Particle, Protein Subunits, Membrane Transport Proteins, Escherichia coli Proteins, Fluorescence Resonance Energy Transfer

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