A single copy of SecYEG is sufficient for preprotein translocation.
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The heterotrimeric SecYEG complex comprises a protein-conducting channel in the bacterial cytoplasmic membrane. SecYEG functions together with the motor protein SecA in preprotein translocation. Here, we have addressed the functional oligomeric state of SecYEG when actively engaged in preprotein translocation. We reconstituted functional SecYEG complexes labelled with fluorescent markers into giant unilamellar vesicles at a natively low density. Förster's resonance energy transfer and fluorescence (cross-) correlation spectroscopy with single-molecule sensitivity allowed for independent observations of the SecYEG and preprotein dynamics, as well as complex formation. In the presence of ATP and SecA up to 80% of the SecYEG complexes were loaded with a preprotein translocation intermediate. Neither the interaction with SecA nor preprotein translocation resulted in the formation of SecYEG oligomers, whereas such oligomers can be detected when enforced by crosslinking. These data imply that the SecYEG monomer is sufficient to form a functional translocon in the lipid membrane.
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The E. coli SecYEG translocon was found to exist as a functional monomer and as a dimer stabilized by cardiolipin.
“The E. coli SecYEG translocon was found to exist as a functional monomer (Menetret et al., 2007; Kedrov et al., 2011; Park and Rapoport, 2012) and as a dimer stabilized by cardiolipin (Gold et al., 2010).”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Kedrov et al., 2011
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Single‐molecule analysis of dynamics and interactions of the SecYEG translocon
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- Authors
- Kedrov, A., Kusters, I., Krasnikov, V. V., & Driessen, A. J. M.
- Affiliations
- University of Groningen (NL)
- Corresponding author
- Driessen, Arnold J M
- Venue
- The EMBO Journal
- Published
- 2011-09-06
- Volume
- 30
- Issue
- 21
- Pages
- 4387-4397
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC3230372
- OpenAlex
- W2134530662
- Cited by
- 74
- References
- 54
- Citations by year
- 2026: 1 · 2024: 3 · 2023: 1 · 2022: 3 · 2021: 3 · 2020: 2 · 2019: 14 · 2018: 1 · 2017: 2 · 2016: 4 · 2015: 11 · 2014: 7 · 2013: 10 · 2012: 10
- FWCI
- 5.58
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (publishedVersion, other-oa)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (submittedVersion)
- Topics
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- SecYEG, preprotein translocation, oligomeric state, translocon, SecA, protein-conducting channel, plasma membrane, single-molecule fluorescence, fluorescence resonance energy transfer, giant unilamellar vesicles, ATP-dependent translocation, bacterial protein secretion
- MeSH terms
- SEC Translocation Channels, Escherichia coli, Membrane Lipids, Membrane Proteins, Models, Biological, Protein Precursors, Methanococcus, Gene Dosage, Protein Transport, Escherichia coli Proteins, Organisms, Genetically Modified, Unilamellar Liposomes, Protein Multimerization
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