YidC, an assembly site for polytopic Escherichia coli membrane proteins located in immediate proximity to the SecYE translocon and lipids.
Open accessAbstract
Like its mitochondrial homolog Oxa1p, the inner membrane protein YidC of Escherichia coli is involved in the integration of membrane proteins. We have analyzed individual insertion steps of the polytopic E. coli membrane protein MtlA targeted as ribosome-nascent chain complexes to inner membrane vesicles. YidC can accommodate at least the first two transmembrane segments of MtlA at the protein lipid interface and retain them even though the length of the nascent chain would amply allow insertion into membrane lipids. An even longer insertion intermediate of MtlA is described that still has the first transmembrane helix bound to YidC while the third contacts SecE and YidC during integration. Our findings suggest that YidC forms a contiguous integration unit with the SecYE translocon and functions as an assembly site for polytopic membrane proteins mediating the formation of helix bundles prior to their release into the membrane lipids.
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For being active in protein transport, the SecYEG translocon depends on the coordinated interaction with multiple partner proteins that select potential SecYEG substrates, provide the driving force for protein transport, coordinate substrate release from the SecYEG channel, and communicate with components of the proteostasis network.
“For being active in protein transport, the SecYEG translocon depends on the coordinated interaction with multiple partner proteins that select potential SecYEG substrates (Lill et al., 1990; van der Does et al., 1996; Angelini et al., 2005), provide the driving force for protein transport (Tsukazaki et al., 2011; Knyazev et al., 2018), coordinate substrate release from the SecYEG channel (Beck et”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Beck et al., 2001
Lateral release of transmembrane domains out of the SecY channel is further facilitated by YidC, which associates with the lateral gate of SecY to form a tetrameric protein channel.
“Lateral release of transmembrane domains out of the SecY channel is further facilitated by YidC (Beck et al., 2001; Houben et al., 2002), which associates with the lateral gate of SecY to form a tetrameric protein channel (Sachelaru et al., 2015, 2017).”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Beck et al., 2001
The intimate contact between the hydrophilic groove of YidC and the lateral gate of SecY provides further support for the concept that TMs leaving the SecY channel are first bound by YidC before they are released into the lipid phase.
“The intimate contact between the hydrophilic groove of YidC and the lateral gate of SecY provides further support for the concept that TMs leaving the SecY channel are first bound by YidC before they are released into the lipid phase (Beck et al., 2001; Houben et al., 2002).”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Beck et al., 2001
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- Authors
- Beck, K., Eisner, G., Trescher, D., Dalbey, R. E., Brunner, J., & Müller, M.
- Affiliations
- University of Freiburg (DE)
- The Ohio State University (US)
- ETH Zurich (CH)
- Corresponding author
- Müller, Matthias
- ORCID
- Brunner, Josef
- Venue
- The EMBO Reports
- Published
- 2001-08-01
- Volume
- 2
- Issue
- 8
- Pages
- 709-714
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- PMC
- PMC1083991
- OpenAlex
- W2162514321
- Cited by
- 171
- References
- 22
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 3 · 2023: 3 · 2022: 3 · 2021: 3 · 2019: 3 · 2018: 4 · 2017: 5 · 2016: 3 · 2015: 6 · 2014: 10 · 2013: 8 · 2012: 7
- FWCI
- 7.83
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- EMBO Reports (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- FreiDok plus (Universitätsbibliothek Freiburg) (submittedVersion)
- Funders
- National Science Foundation
- European Commission
- 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 › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- YidC, polytopic membrane proteins, membrane insertion, SecE, ribosome-nascent chain complex, lipid interfaces, Escherichia coli inner membrane
- MeSH terms
- Bacterial Proteins, Escherichia coli, Membrane Lipids, Membrane Proteins, Monosaccharide Transport Proteins, Phosphoenolpyruvate Sugar Phosphotransferase System, Protein Biosynthesis, Membrane Transport Proteins, Escherichia coli Proteins
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