The DOI matches its Crossref record; 402 of the 402 references it cites were found in a registry or an index.
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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“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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“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
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“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
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Cites
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Cited by
Sorted by citations
The Sec translocon mediated protein transport in prokaryotes and eukaryotes.
Denks, K., Vogt, A., Sachelaru, I., Petriman, N.-A., Kudva, R., & Koch, H.-G. (2014) · Molecular Membrane Biology · doi:10.3109/09687688.2014.907455 · Cited by 170
Self-citationChaperone networking facilitates protein targeting to the bacterial cytoplasmic membrane.
Castanié-Cornet, M.-P., Bruel, N., & Genevaux, P. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.11.007 · Cited by 129
Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon
Jomaa, A., Boehringer, D., Leibundgut, M., & Ban, N. (2016) · Nature Communications · doi:10.1038/ncomms10471 · Cited by 115
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
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
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
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
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
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
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
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
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
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
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Metadata
- 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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