Protein translocation across the inner membrane of Gram-negative bacteria: the Sec and Tat dependent protein transport pathways.
Open accessAbstract
Gram negative bacteria possess a large variety of protein transport systems, by which proteins that are synthesised in the cytosol are exported to destinations in the cell envelope or entirely secreted into the extracellular environment. The inner membrane (IM) contains three major transport systems for the translocation and insertion of signal sequence containing proteins: the Sec translocon, the YidC insertase, and the Tat system. The heterotrimeric SecYEG translocon forms a narrow channel in the membrane that serves a dual function; it allows the translocation of unfolded proteins across the pore and the integration of α-helical proteins into the IM. The YidC insertase is a multi-spanning membrane protein that cooperates with the SecYEG translocon during the integration of membrane proteins but also functions as an independent insertase. Depending upon the type of protein cargo that needs to be transported, the Signal Recognition Particle (SRP), the SRP receptor, SecA and chaperones are required to coordinate translation with transport and to target and energise the different transport systems. The Tat system consists of three membrane proteins (TatA, TatB and TatC) which in a still unknown manner accomplish the transmembrane passage of completely folded proteins and protein complexes.
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The SecYEG translocon is universally conserved and mediates the translocation of newly synthesized proteins into and across the cytoplasmic membrane.
“The universally conserved SecYEG translocon acts at the center of bacterial protein transport and mediates the translocation of newly synthesized proteins into and across the cytoplasmic membrane.”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Kudva et al., 2013
In E. coli, SecA is present in about 2,000-5,000 copies per cell and is much more abundant than the SecYEG complex, which exists in about 500 copies.
“In E. coli it is present in about 2,000–5,000 copies per cell (Kudva et al., 2013; Smets et al., 2019) and therefore much more abundant than the SecYEG complex, which exists in about 500 copies (Kudva et al., 2013).”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Kudva et al., 2013
FtsY and SecA have comparable affinities for the SecYEG translocon and are present in comparable copy numbers in E. coli.
“FtsY and SecA have comparable affinities for the SecYEG translocon and are present in comparable copy numbers in E. coli (Douville et al., 1995; Kudva et al., 2013; Kuhn et al., 2015)”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Kudva et al., 2013
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- Kuhn, P., Kudva, R., Welte, T., Sturm, L., Koch, H.G., 2013. In: Fronzes, R., Remault, H. (Eds.), Targeting and Integration of Bacterial Membrane Proteins. Bacterial Membranes, Structure and Molecular Biology. Horizon Scientific Press. in press.
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Oswald, J., Njenga, R., Natriashvili, A., Sarmah, P., & Koch, H.-G. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.664241 · Cited by 88 · see citing works
Self-citationCo-translational protein targeting in bacteria.
Steinberg, R., Knüpffer, L., Origi, A., Asti, R., & Koch, H.-G. (2018) · FEMS Microbiology Letters · doi:10.1093/femsle/fny095 · Cited by 81 · see citing works
Self-citationPetriman, N.-A., Jauß, B., Hufnagel, A., Franz, L., Sachelaru, I., Drepper, F., Warscheid, B., & Koch, H.-G. (2018) · Scientific Reports · doi:10.1038/s41598-017-19019-w · Cited by 66 · see citing works
Self-citationYidC and SecYEG form a heterotetrameric protein translocation channel.
Sachelaru, I., Winter, L., Knyazev, D. G., Zimmermann, M., Vogt, A., Kuttner, R., Ollinger, N., Siligan, C., Pohl, P., & Koch, H.-G. (2017) · Scientific Reports · doi:10.1038/s41598-017-00109-8 · Cited by 58 · see citing works
Self-citationJauss, B., Petriman, N.-A., Drepper, F., Franz, L., Sachelaru, I., Welte, T., Steinberg, R., Warscheid, B., & Koch, H.-G. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010686 · Cited by 43 · see citing works
Self-citationDynamic interaction of the Sec Translocon with the chaperone PpiD.
Sachelaru, I., Petriman, N.-A., Kudva, R., & Koch, H.-G. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.577916 · Cited by 37 · see citing works
Self-citationThe bacterial SRP receptor, FtsY, is activated on binding to the translocon.
Draycheva, A., Bornemann, T., Ryazanov, S., Lakomek, N., & Wintermeyer, W. (2016) · Molecular Microbiology · doi:10.1111/mmi.13452 · Cited by 34 · see citing works
Posttranslational insertion of small membrane proteins by the bacterial signal recognition particle.
Steinberg, R., Origi, A., Natriashvili, A., Sarmah, P., Licheva, M., Walker, P. M., Kraft, C., High, S., Luirink, J., Shi, W. Q., et al. (2020) · PLOS Biology · doi:10.1371/journal.pbio.3000874 · Cited by 34 · see citing works
Self-citationMolecular mimicry of SecA and signal recognition particle binding to the bacterial ribosome.
Knüpffer, L., Fehrenbach, C., Denks, K., Erichsen, V., Petriman, N.-A., & Koch, H.-G. (2019) · mBio · doi:10.1128/mbio.01317-19 · Cited by 28 · see citing works
Self-citationInvolvement of PpiD in Sec-dependent protein translocation.
Fürst, M., Zhou, Y., Merfort, J., & Müller, M. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.10.012 · Cited by 26 · see citing works
Self-citation
- Authors
- Kudva, R., Denks, K., Kuhn, P., Vogt, A., Müller, M., & Koch, H.-G.
- Affiliations
- University of Freiburg (DE)
- Corresponding author
- Müller, Matthias
- Koch, Hans-Georg
- Venue
- Research in Microbiology
- Publisher
- Elsevier BV
- Published
- 2013-07
- Volume
- 164
- Issue
- 6
- Pages
- 505-534
- ISSN
- 0769-2609 (ISSN-L)
- 0923-2508
- OpenAlex
- W1979649414
- Cited by
- 177
- References
- 402
- Citations by year
- 2026: 5 · 2025: 9 · 2024: 6 · 2023: 10 · 2022: 13 · 2021: 12 · 2020: 14 · 2019: 14 · 2018: 11 · 2017: 14 · 2016: 16 · 2015: 29 · 2014: 18 · 2013: 6
- FWCI
- 15.26
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Research in Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (GSC‐4, FOR 967, SFB-746, FOR 929)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- protein translocation, Gram-negative bacteria, inner membrane, Sec translocon, Tat system, SecYEG translocon, signal recognition particle, SecA, molecular chaperones, membrane protein insertion, protein secretion, TatA, TATB, TatC
- MeSH terms
- Bacterial Proteins, Cell Membrane, Gram-Negative Bacteria, Protein Transport, Bacterial Secretion Systems
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