Research group of Hans-Georg Koch
Research
Our work is focused on protein transport and protein assembly mechanisms in bacterial cells.
Bacteria like eukaryotic cells have to export a large subset of the cytosolically synthesized proteins into the inner membrane, the periplasmic space, the outer membrane or the extracellular space. To achieve this, bacteria have developed highly specific and highly sophisticated protein transport machineries.
Some of these pathways are found in bacteria only and are crucial determinants for bacterial pathogenicity; other pathways were originally “invented” by prokaryotes but have been conserved also in higher eukaryotes. Therefore bacteria are perfect model organisms for studying the molecular details of these essential processes.

Funding
The Koch research group receives research funding from the following funding programs of the German Research Foundation (Deutsche Forschungsgemeinschaft, DFG)
- Collaborative Research Centre (CRC) 1381: Protein Machineries since 2019, extended 2023
- Cluster of Excellence CIBSS – Centre for Integrative Biological Signalling Studies since 2019
- Priority program (Schwerpunktprogram, SPP) 2002: Small Proteins – an Unexplored World since 2017
- Research Training Group (RTG) 2202: Transport across and into membranes 2016-2025
Team

CV Hans-Georg Koch
Seit 2012 | Member Executive Board and Vice-Director ‘Spemann Graduate School of Biology and Medicine’ |
Seit 2009 | Professor of Biochemistry and Molecular Biology |
2003 ‑ 2008 | Senior Lecturer (Hochschuldozent) and group leader at the Institute of Biochemistry and Molecular Biology, University of Freiburg |
2002 | Habilitation for Biochemistry and Molecular Biology at the Medical Faculty, University of Freiburg |
2001 ‑ 2002 | Assistenzprofessor (Habilitation) am Institut für Biochemie und Molekularbiologie, University of Freiburg |
1997 ‑ 2000 | Postdoc in the group of Matthias Müller at the Institute of Biochemistry and Molecular Biology, University of Freiburg |
1994 ‑ 1997 | NIH-fellow in the group of Fevzi Daldal at the Leidy Laboratory of Biology, University of Pennsylvania, Philadelphia |
1991 ‑ 1994 | PhD Thesis in the Lab of J.H. Klemme at the Institute of Microbiology and Biotechnology, Rhein. Friedrich-Willhelm University Bonn (supported by a PhD fellowship of the “Studienstiftung des Deutschen Volkes”) |
1990 ‑ 1991 | Diploma Thesis in the Lab of J.H. Klemme at the Institute of Microbiology and Biotechnology, Rhein. Friedrich-Willhelm University Bonn |
Publications
Czech L, Mais CN, Sarmah P, Krazat H, Giammarinaro P, Freibert S, Musial J, Bernningshausen O., Steinchen W, Beckmann R, Koch HG, Bange, G. (2022) Shutdown of secretory pathway by the bacterial alarmones (p)ppGpp. Nature Commun. 13:1069. doi: 10.1038/s41467-022-28675-0.
Steinberg R, Origi A, Natriashvili A, Sarmah P, Licheva M, Walker PM, Kraft C, High S, Luirink J, Shi, WQ, Helmstädter M, Ulbrich MH, and Koch HG (2020) Post-translational insertion of small membrane proteins by the bacterial signal recognition particle. PloS Biology 18(9), e30000874, doi: 10.1371/journal.pbio.3000874.
Marckmann D, Trasnea PI, Schimpf J, Winterstein C, Andrei A, Schmollinger S, Blaby-Haas CE, Friedrich T, Daldal F, Koch HG (2019) The cbb3-type cytochrome oxidase assembly factor CcoG is a widely distributed cupric reductase. Proc. Natl. Acad. Sci. USA 116, 21166-21175 doi: 10.1073/pnas.1913803116.
Jauss B, Petriman NA, Drepper F, Franz L, Steinberg R, Warscheid B, Koch HG (2019) Non-competitive binding of PpiD and YidC to the SecYEG translocon expands the global view on the SecYEG interactome in E. coli. J. Biol. Chem. 294, 19167-19183 doi: 10.1074/jbc.RA119.010686.
Sachelaru, I., Winter, L., Knyazev, D., Zimmermann, M., Vogt, A., Kuttner, R., Ollinger, N., Siligan, C., Pohl, P., and Koch, H.G.(2017). YidC and SecYEG form a heterotetrameric protein translocation channel. Sci. Rep. 7, 101.
Denks, K., Sliwinski, N., Erichsen, V., Borodkina, B., Origi, A., and Koch, H.G. (2017). The signal recognition particle contacts uL23 and scans substrate translation inside the ribosomal tunnel. Nat. Microbiol. 2, 16215.
Braig, D., Nero, T., Koch, H.G., Kaiser, B., Wang, X., Thiele, J.R., Morton, C., Zeller, J., Kiefer, J., Potempa, L.A., Mellett, N.A., Miles, L.A., Du, X., Meikle, P.J., Huber-Lang, M., Stark, G.B., Parker, M.W., Peter, K., and Eisenhardt, S.U. (2017). Transitional changes in the CRP structure lead to the exposure of pro-inflammatory binding sites. Nat. Commun. 8, 14188.
Kuhn, P., Draycheva, A., Vogt, A., Petriman, N.A., Sturm, L., Drepper, F., Warscheid, B., Wintermeyer, W., and Koch, H.G.(2015). Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon. J. Cell Biol.211, 91-104.
Angelini, S., Deitermann, S., and Koch, H.G. (2005). FtsY, the bacterial SRP receptor functionally and physically interacts with the SecYEG translocon. EMBO Rep. 6, 476-481.
Alami, M., Lüke, I., Deitermann, S., Eisner, G., Koch, H.G., Brunner, J., and Müller, M. (2003). Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli. Mol. Cell 12, 937-946.
Neumann-Haefelin, C., Schäfer, U., Müller, M., and Koch, H.G. (2000). SRP-dependent cotranslational targeting and SecA-dependent translocation analyzed as individual step in the export of a bacterial protein. EMBO J. 19, 6419-6426.
Jiang, H., Milanov, M., Jüngert, G., Angebauer, L., Flender, C., Smudde, E., Gather, F., Jessen H.J., Koch, H.G. (2024). Control of a chemical chaperone by a universally conserved ATPase. iScience. doi: 10.1016/j.isci.2024.110215
Karari Njenga, R., Boele, J., Drepper, F., Sinha, K., Marouda, E., Huesgen, P. F., Blaby-Haas, C., and Koch, H.G. (2024). Ribosome inactivation by a class of widely distributed C-tail anchored membrane proteins. Structure. doi.org/10.1016/j.str.2024.09.019
Leinberrger, F.H., Cassidy, L., Edelmann, D., Schmid, N.E., Oberpaul, M., Blumenkamp, P., Schmidt, S., Natriashvili, A., Ulbrich, M.H., Tholey, A., Koch, H.G., and Berghoff, B.A. (2024). Protein aggregation is a consequence of the dormancy-inducing membrane toxin TisB in Escherichia coli. mSystems. doi:10.1128/msystems.01060-24
Zmyslia, M., Capper, M.J., Grimmeisen, M., Sartory, K., Deuringer, B., Abdelsalam, M., Shen, K., Jung, M., Sippl, W., Koch, H.G., Kaul, L., Süss, R., Köhnke, J., and Jessen-Trefzer, C. (2024). A nanoengineered tandem nitroreductase: designing a robust prodrug-activating nanoreactor. RCS Chemical Biology. doi: 10.1039/d4cb00127c
Rauch, J., Kurscheidt, K., Shen, K., Andrei, A., Daum, N., Öztürk, Y., Melin, F., Layer, G., Hellwig, P., Daldal, F., and Koch. H.G. (2024). The small membrane protein CcoS is involved in cofactor insertion into cbb3-type cytochrome oxidase. BBA Bioenergetics. doi: 10.1016/j.bbabio.2024.149524
Shang, W., Lichtenberg, E., Mlesnita, A.M., Wilde, A., and Koch, H.-G. (2024). The contribution of mRNA targeting to spatial protein localization in bacteria. FEBS J. doi: 10.1111/febs.17054
- Knyazev, D., Winter, L., Vogt, A., Posch, S., Öztürk, Y., Siligan, C., Goessweiner-Mohr, N., Hagleitner-Ertugrul., Koch, H.G., and Pohl, P. (2023). YidC from Escherichia coli forms an ion-conducting pore upon activation by ribosomes. Biomolecules. dot: https://doi.org/10.3390/biom13121774
- Öztürk, Y, Andrei, A, Blaby-Haas, CE, Daum, N, Daldal, F, Koch H. G. (2023). Metabolic sensing of extracytoplasmic copper availability via translational control by a nascent exported protein. mBio. doi: 10.1128/mbio.03040-22.
- Sarmah, P., Shang, W., Origi A., Licheva, M., Kraft, C., Ulbrich, M., Lichtenberg, E., Wilde, A., Koch H.G. (2023). mRNA targeting eliminates the need for the signal recognition particle during membrane protein insertion in bacteria. Cell reports. doi: 10.1016/j.celrep.2023.112140
- Fielden, L.F, Busch, J.D., Merkt, S.G., Ganesan, I., Steiert, C., Hasselblatt, H., Busto, J.V., Wirth, C., Zufall, N., Jungbluth, S., Noll, K., Dung, J.M., Butenko, L., Malsburg, v.d.K., Koch, H.G., Hunte, C., Laan, v.d. M., and Wiedemann, N. (2023). Central role of Tim17 in mitochondrial presequence protein translocation. Nature
- Njenga, R., Boele, J. Öztürk, Y., and Koch, H.-G. (2023). Coping with stress: How bacteria fine-tune protein synthesis and protein transport. J. Biol. Chem.
- Vögtle, N.F., Koch, H.-G., and Meisinger, C. (2022), A common evolutionary origin reveals fundamental principles of protein insertases. PlosBiology 20(3):e3001558. doi: 10.1371/journal.pbio.3001558
- Czech L, Mais CN, Sarmah P, Krazat H, Giammarinaro P, Freibert S, Musial J, Bernningshausen O., Steinchen W, Beckmann R, Koch HG, Bange, G. (2022) Shutdown of secretory pathway by the bacterial alarmones (p)ppGpp. Nature Commun. 13:1069. doi: 10.1038/s41467-022-28675-0.
- Carabadjac, I, Natriashvili, A., Koch, H.G., Heerklotz, H. (2022) Exploring protein-dependent changes of the properties of bio-membranes using time-resolved fluorescence. Biophysical Journal 121(3)11
- Tsypik, O., Makitrynskyy, R., Yan, X., Koch, H.-G., Paulutat, T. and Bechthold, A (2021) Regulatory control of Rishirilide(s) biosynthesis in Streptomyces bottropensis. Microorganisms 9(2):374
- Steenhuis, M., Konigstein, G.M., Oswald, J., Pick, T., O`Keefe, S., Koch, H.-G., Cavalie, A., Whitehead, R.C., Swanton, E., High, S. and Luirink, J. (2021) Eeyarestatin 24 impairs SecYEG-dependent protein trafficking and inhibits growth of clinically relevant pathogens. Mol. Microbiology 115, 28-40, doi: 10.1111/mmi.14589
- Landwehr, V., Milanov, M., Angebauer, L., Jüngert, G., Hiersemenzel, A., Schmitt, F., Jiang, H. Öztürk, Y., Dannenmeier, S., Drepper, F., Warscheid, B. and Koch. H.-G. (2021). The universally conserved ATPase YchF regulates the translation of leaderless mRNAs in response to stress conditions. Front. Mol. Biosciences 8, 643696; doi: 10.3389/fmolb.2021.643696
- Khalfaoui-Hassani, B., Trasnea, P.I., Steimle, S., Koch, H.-G. and Daldal F. (2021) Cysteine Mutants of the Major Facilitator Superfamily-Type Transporter CcoA Provide insight into Copper Import. mBio 12(4), e0156721; doi: 10.1128/mBio.01567-21
- Wang, X.; Bittner, T.; Milanov, M.; Kaul, L.; Mundinger, S.; Koch, H.-G..; Jessen-Trefzer, C.; and Jessen, H. (2021). Pyridinium modified anthracenes and their endoperoxides provide a tunable scaffold with activity against gram-positive and gram-negative bacteria. ACS Infectious Diseases 7(8), 2073-2080; doi: 10.1021/acsinfecdis.1c00263
- Agne, M., Estelmann, S., Seelmann, C., Kung, J., Wilkens, D., Koch, H.-G., van der Does, C., Albers, S., von Ballmoos, C., Simon, J., and Boll, M. (2021). The missing enzymatic link in syntrophic methane formation from fatty acids. Proc. Natl. Acad. Sci. USA 118(40), e2111682118; doi: 10.1073/pnas.2111682118.
- Dannenmaier, S., Desroche-Altamirano, C., Schüler, L., Zhang, Y., Hummel, J., Oeljeklaus, S., Koch, H.-G., Rospert, S., Alberti, S. and Warscheid, B. (2021). Quantitative proteomics identifies the universally conserved ATPase Ola1p as a positive regulator of heat shock response in Saccharomyces cerevisiae. J. Biol. Chem. 297(5),101050, doi: 10.1016/j.jbc.2021
- Andrei, A., di Renzo, A.M., Öztürk, Y., Meisner, A., Daum, N., Frank, F., Rauch, J., Daldal, F., Andrade, S., and Koch, H.G. (2021). The CopA2-type P1B –type ATPase CcoI serves as central hub for cbb3-Cox biogenesis. Frontiers in Microbiology 12,712465; doi: 10.3389/fmicb.2021.712465
- Öztürk, Y., Blaby-Haas, C.E., Daum, N., Andrei, A., Daldal, F. and Koch, H.G. (2021) Maturation of Rhodobacter capsulatus Multicopper Oxidase CutO Depends on the CopA Copper Efflux Pathway and requires the cutF Product. Frontiers in Microbiology 12:720644; doi: 10.3389/fmicb.2021.720644.
- Steinberg, R. and Koch, H.-G. (2021) The largely unexplored biology of small proteins in pro- and eukaryotes. FEBS J. 288(24):7002-7024; doi: 10.1111/febs.15845
- Oswald, J., Njenga, R., Natriashvili, A., Sarmah, P., and Koch, H.-G. (2021) The dynamic Sec translocon. Frontiers Mol. Biosciences 8, 664241; doi: 10.3389/fmolb.2021.664241
- Landwehr, V., Milanov, M., Jiang, H. and Koch, H.G. (2021) The role of the universally conserved ATPase YchF/Ola1 in translation regulation during cellular stress. Microorganisms
- Selamoglu, N., Önder, Ö., Öztürk, Y., Khalfaoui-Hassani, B., Blaby-Haas, C.B., Garcia, B., Koch, H.-G. and Daldal, F. (2020) Comparative Differential Cuproproteomes of Rhodobacter capsulatus Reveal Novel Copper Homeostasis Related Proteins. Metallomics, 12, 572-591
- Haas TM, Qiu D, Häner M, Angebauer L, Ripp A, Singh J, Koch HG, Jessen-Trefzer C, Jessen HJ. (2020) Four Phosphates at One Blow: Access to Pentaphosphorylated Magic Spot Nucleotides and Their Analysis by Capillary Electrophoresis. J. Org. Chem., doi: 10.1021/acs.joc.0c00841
- Steenhuis, M., Konigstein, G.M., Oswald, J., Pick, T., O`Keefe, S., Koch, H.-G., Cavalie, A., Whitehead, R.C., Swanton, E., High, S. and Luirink, J. (2020) Eeyarestatin 24 impairs SecYEG-dependent protein trafficking and inhibits growth of clinically relevant pathogens. Mol. Microbiology, doi: 10.1111/mmi.14589
- Steinberg, R., Origi, A., Natriashvili, A., Sarmah, P., Licheva, M., Walker, P.M., Kraft, C., High, S., Luirink, J., Shi, W.Q., Helmstädter, M., Ulbrich, M.H., and Koch, H.-G. (2020) Post-translational insertion of small membrane proteins by the bacterial signal recognition particle. Plos Biology, doi: 10.1371/journal.pbio.3000874
- Jung, S., Bader, V., Natriashvili, A., Koch, H.-G., Winklhofer, K.F., and Tatzelt, J (2020) SecY mediated quality control prevents translocation of non-gated porins. Scientific reports, doi: 10.1038/s41598-020-73185-y
- Andrei, A., Öztürk, Y., Khalfaoui-Hassani, B., Rauch, J., Marckmann, D., Trasnea, PI, Daldal, F., and Koch, H.-G. (2020) Cu homeostasis in Bacteria: The Ins and Outs. Membranes 10(9), e242
- Simunovic, F., Winninger, O., Strassburg, S., Koch, H.-G., Finkenzeller, G., Stark, B.G. and Lampert, F. (2019). Increased differentiation and production of extracellular matrix components of priamry human osteoblasts after co-cultivation with endothelial cells: A quantitative proteomics approach. J. Cellular Biochem. 120(1):396-404.
- Utz, M. Andrei, A., Milanov, M., Trasnea, PI, Marckmann, D., Daldal, F., Koch, H.-G. (2019) The Cu chaperone CopZ is required for Cu homeostasis in Rhodobacter capsulatus and influences cytochrome cbb3 oxidase assembly. Mol Microbiology 111(3):764-783.
- Zhang, Y., Blaby-Haas, C.E., Steimle, S., Verissimo, A.F., Garcia-Angulo, V., Koch, H.G., Daldal, F., Khalfaoui-Hassani, B (2019) Cu Transport by the Extended Family of CcoA-like Transporters (CalT) in Proteobacteria. Scientific reports 9:1208
- Knüpffer, L., Fehrenbach, C., Denks, K., Erichsen, V., Petriman, N.A., Koch, H.-G. (2019) Molecular mimicry of SecA and signal recognition particle binding to the bacterial ribosome. mBio 10, e01317-19
- Marckmann, D., Trasnea, P.I, Schimpf, J., Winterstein, C., Andrei, A., Schmollinger, S., Blaby-Haas, C.E., Friedrich, T., Daldal, F., Koch, H.-G. (2019) The cbb3-type cytochrome oxidase assembly factor CcoG is a widely distributed cupric reductase. Proc. Natl. Acad. Sci. USA, 116, 21166-21175
- Jauss, B., Petriman, N.A., Drepper, F., Franz, L. Steinberg, R., Warscheid, B. Koch, H.-G, (2019) Non-competitive binding of PpiD and YidC to the SecYEG translocon expands the global view on the SecYEG interactome in E. coli. J. Biol. Chem. 294, 19167-19183
- Origi, A., Natriashvili, A., Knüpffer, L., Fehrenbach, C., Denks, K., Asti, R., Koch, H.-G. (2019) Yet another role for the bacterial ribosome. Microbial Cell 6, 524-526
- Petriman, N.A., Jauss, B., Hufnagel, A., Franz, L., Sachelaru, I., Drepper, F., Warscheid, B., and Koch, H-G. (2018) The interaction network of the YidC insertase with the SecYEG translocon, SRP and the SRP receptor FtsY. Scientific reports 8, 578
- Khalfaoui-Hassani, B., Wu, H., Blaby-Haas, C., Zhang, Y., Sandri, F., Verissimo, A.F., Koch, H.-G., and Daldal, F. (2018). Widespread Distribution and Functional Specificity of the Copper Importer CcoA: Distinct Cu Uptake Routes for Bacterial Cytochrome c Oxidases. mBIO 9, e00065-18
- Trasnea, P.I., Andrei, A., Markmann, D., Utz, M., Khalfaoui-Hassani, B.; Selamoglu, N., Daldal, F., and Koch, H.G. (2018). A copper relay system involving two periplasmic chaperones drives cbb3 type cytochrome c oxidase biogenesis in Rhodobacter capsulatus. ACS Chemical Biology 13, 1388-1397.
- Steinberg, R., Knüpffer, L., Origi, A., Asti, R. and Koch, H.G. (2018) Co-translational protein targeting in bacteria. FEMS Microbiol. Lett. 365(11): 10.1093 Thematic Series on Bacterial Protein Export.
- Simunovic, F., Winninger, O., Strassburg, S., Koch, H.-G., Finkenzeller, G., Stark, B.G. and Lampert, F. (2018). Increased differentiation and production of extracellular matrix components of priamry human osteoblasts after co-cultivation with endothelial cells: A quantitative proteomics approach. J. Cellular Biochem. doi: 10.1002/jcb.27394.
- Zhang, Y., Blaby-Haas, C.E., Steimle, S., Verissimo, A.F., Garcia-Angulo, V., Koch, H.G., Daldal, F., Khalfaoui-Hassani, B. (2018). Cu Transport by the Extended Family of CcoA-like Transporters (CalT) in Proteobacteria. Scientific reports, in press
- Utz, M. Andrei, A., Milanov, M., Trasnea, PI, Marckmann, D., Daldal, F., Koch, H.-G. (2018). The Cu chaperone CopZ is required for Cu homeostasis in Rhodobacter capsulatus and influences cytochrome cbb3 oxidase assembly. Mol Microbiology, in press
2017
Gonsberg, A., Jung, S., Ulbrich, S., Origi, A., Ziska, A., Baier, M., Koch, H.G., Zimmermann, R., Winklhofer, K.F., and Tatzelt, J. (2017) The Sec61/SecY complex is inherently deficient in translocating intrinsically disordered proteins. J. Bio. Chem., 292, 21383-21396
Onder, O., Verissimo, A., Khalfaoui-Hassani, B., Peters, A., Koch, H.-G. and Daldal, F. (2017) Absence of thiol-disulfide oxidoreductase DsbA impairs cbb3-type cytochrome c oxidase biogenesis in Rhodobacter capsulatus. Frontiers in Microbiology, 8, 2576
David Braig, Tracy L. Nero, Hans-Georg Koch, Benedict Kaiser, Xiaowei Wang, Jan R. Thiele, Craig Morton, Johannes Zeller, Jurij Kiefer, Lawrence A.Potempa, Natalie A. Mellett, Luke A. Miles, Xiao-Jun Du, Peter J. Meikle, Markus Huber-Lang, G. Björn Stark, Michael W. Parker, Karlheinz Peter, Steffen U. Eisenhardt (2017) Transitional changes in the CRP structure lead to the exposure of pro-inflammatory binding sites.Nature communications 8, 14188
Denks, K., Sliwinski, N., Erichsen, V., Borodkina, B., Origi, A. and Koch, H.G. (2017)The signal recognition particle contacts uL23 and scans substrate translation inside the ribosomal tunnel accepted by Nature Microbiology, 2, 16265
Sachelaru, I., Winter, L., Knyazev, D., Zimmermann, M., Vogt, A., Kuttner, R., Ollinger, N., Siligan, C., Pohl, P. and Koch, H.G. (2017) YidC and SecYEG form a heterotetrameric protein translocation channel. Scientific reports, in press
Dalbey, R.E., Koch, H.G., and Kuhn A. (2017) Targeting and insertion of membrane proteins. EcoSal, in press.
2016
Hannemann L, Suppanz I, Ba Q, MacInnes K, Drepper F, Warscheid B, Koch HG: Redox Activation of the Universally Conserved ATPase YchF by Thioredoxin 1. Antioxid Redox Sign, 2016; 24 (3) : 141-156: http://dx.doi.org/10.1089/ars.2015.6272
Khalfaoui-Hassani B, Verissimo AF, Koch HG, Daldal F: Uncovering the Transmembrane Metal Binding Site of the Novel Bacterial Major Facilitator Superfamily-Type Copper Importer CcoA. Mbio, 2016; 7 (1) : e01981-e01915: http://dx.doi.org/10.1128/mBio.01981-15
Trasnea PI, Utz M, Khalfaoui-Hassani B, Lagies S, Daldal F, Koch HG: Cooperation between two periplasmic copper chaperones is required for full activity of the cbb3 -type cytochrome c oxidase and copper homeostasis in Rhodobacter capsulatus. Mol Microbiol, 2016; 100 (2) : 345-361: http://dx.doi.org/10.1111/mmi.13321
Trasnea, P.I., Marckmann, D., Utz, M., Koch, H.G. (2016) Measurement of cellular copper by Atomic absorption spectroscopy. Bio-protocols, 6, e1948
Khalfaoui-Hassani B, Verissimo, A.F, Shroff, N.P, Ekici, S, Trasnea, P.I, Utz, M, Koch, H.G, Daldal, F: Biogenesis of cytochrome c complexes: from Insertion of Redox Cofactors to Assembly of different subunits. In: Cytochromes and Cytochrome complexes: Structure and Function. In: Advances in Photosynthesis and Respiration Springer, Dordrecht, The Netherlands., 2016
Koch HG, Schneider D: Assembly of Transmembrane b-type Cytochromes and Cytochrome complexes. In: Advances in Photosynthesis and Respiration Springer, Dordrecht, The Netherlands., 2016
2015
Sachelaru, I., Petriman, N.A., Kudva, R., Kuhn, P., Welte, T., Knapp, B., Drepper, F., Warscheid, B., and Koch, H.G. (2015). YidC occupies the lateral gate of the SecYEG translocon and is sequentially displaced by a nascent membrane protein. J. Biol. Chem. 290, 14492
Kuhn, P., Draycheva, A., Vogt, A., Petriman, N.A., Sturm, L., Drepper, F., Warscheid, B., Wintermeyer, W., and Koch, H.G. (2015) Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon. J. Cell Biol. 211, 91-104
Hannemann, L. Suppanz, I., Ba, Q., MacInnes, K., Drepper, F., Warscheid, B., and Koch, H.G. (2015) Redox-activation of the universally conserved ATPase YchF by thioredoxin 1. Antioxidants and Redox Signaling, in press.
Khalfaoui-Hassani, B., Versissimo, A.F., Koch, H.G., and Daldal, F. (2015) Uncovering the Transmembrane metal binding site of the novel MFS-type copper importer CcoA. Mbio in press
Trasnea, P.I., Utz, M., Khalfaoui-Hassani, B., Lagies, S., Daldal, F. and Koch, H.G. (2015) Cooperation between two periplasmic copper chaperones is required for full activity of the cbb3-type cytochrome c oxidase and copper homeostasis in Rhodobacter capsulatus. Mol. Microbiology in press
Petriman, N.A., Jauß, B. and Koch, H.G. (2015) Proteintransport in Bakterien: Einblicke in die Funktionsweise komplexer Transportmaschinerien. Biospektrum 7, 696-698
2014
Ekici, S, Turkarslan, S., Pawlik, G., Dancis, A., Baliga, N.S., Koch, H.G., and Daldal, F. (2014) Intracytoplasmic Copper Homeostasis Controls Cytochrome c Oxidase Production. mBio 5(1) e01055-13
Braig, D., Kaiser, B., Thiele J.R., Bannasch, H., Peter, K., Stark, B., Koch, H.G., Eisenhardt, S.U. (2014) A conformational change of C-reactive protein in burn wounds unmasks its pro-inflammatory properties. Internat. Immunity 26, 467-478
Sachelaru, I., Petriman, N.A., Kudva, R. and Koch, H.G. (2014) Dynamic interaction of the Sec translocon with the periplasmic chaperone PpiD. J. Biol. Chem. 289.21706-21715
Denks, K., Vogt, A.; Sachelaru, I., Petriman, N.A. Kudva, R. and Koch, H.G. (2014). The Sec translocon mediated protein transport in prokaryotes and eukaryotes. Mol. Membrane Biology, 31, 58-84
Koch, H.G. and Schneider, D. (2014). Biogenesis of membrane-bound b-type cytochromes. In: Advances in Photosynthesis and Respiration, Vol. 38; Cytochrome and Cytochrome complexes. (Cramer, W.A. & Kallas, T., Eds). Springer, Dordrecht.
Koch, H.G. and Daldal, F. (2014). Biogenesis of cbb3-type cytochrome oxidases. In: Cytochromes and Cytochrome complexes: Structure and Function. Advances in Photosynthesis and Respiration, Vol. 38; Cytochrome and Cytochrome complexes. (Cramer, W.A. & Kallas, T., Eds). Springer, Dordrecht.
2013
Ekici S, Jiang X, Koch HG, Daldal F: Missense mutations in cytochrome c maturation genes provide new insights into Rhodobacter capsulatus cbb3-type cytochrome c oxidase biogenesis. J Bacteriol, 2013; 195 (2) : 261-269: http://dx.doi.org/10.1128/JB.01415-12
Kudva R, Denks K, Kuhn P, Vogt A, Muller M, Koch HG: Protein translocation across the inner membrane of Gram-negative bacteria: the Sec and Tat dependent protein transport pathways. Res Microbiol, 2013; 164 (6) : 505-534: http://dx.doi.org/10.1016/j.resmic.2013.03.016
Sachelaru I, Petriman NA, Kudva R, Kuhn P, Welte T, Knapp B, Drepper F, Warscheid B, Koch HG: YidC occupies the lateral gate of the SecYEG translocon and is sequentially displaced by a nascent membrane protein. J Biol Chem, 2013; 288 (23) : 16295-16307: http://dx.doi.org/10.1074/jbc.M112.446583
Koch HG: Keine Pause bei Prolinen: Wie der Elongationsfaktor EF-P die Proteinsynthese rettet Biospektrum, 2013; 3 (13) : 13-13
Kuhn P, Kudva R, Welte T, Sturm L, Koch HG: Targeting and integration of bacterial membrane proteins. In: Remaut H,,Franzes R (Hrsg): Bacterial membranes: Structural an Molecular Biology Horizon Press, 2013
2012
Ekici S, Yang H, Koch HG, Daldal F: Novel transporter required for biogenesis of cbb3-type cytochrome c oxidase in Rhodobacter capsulatus. Mbio, 2012; 3 (1) : 1-11: http://dx.doi.org/10.1128/mBio.00293-11
Lohmeyer E, Schroder S, Pawlik G, Trasnea PI, Peters A, Daldal F, Koch HG: The ScoI homologue SenC is a copper binding protein that interacts directly with the cbb(3)-type cytochrome oxidase in Rhodobacter capsulatus. Bba-bioenergetics, 2012; 1817 (11) : 2005-2015: http://dx.doi.org/10.1016/j.bbabio.2012.06.621
Welte T, Kudva R, Kuhn P, Sturm L, Braig D, Muller M, Warscheid B, Drepper F, Koch HG: Promiscuous targeting of polytopic membrane proteins to SecYEG or YidC by the Escherichia coli signal recognition particle. Mol Biol Cell, 2012; 23 (3) : 464-479: http://dx.doi.org/10.1091/mbc.E11-07-0590
Wenk M, Ba Q, Erichsen V, Macinnes K, Wiese H, Warscheid B, Koch HG: A Universally Conserved ATPase Regulates the Oxidative Stress Response in Escherichia coli. J Biol Chem, 2012; 287 (52) : 43585-43598: http://dx.doi.org/10.1074/jbc.M112.413070
Ekici S, Pawlik G, Lohmeyer E, Koch HG, Daldal F: Biogenesis of cbb(3)-type cytochrome c oxidase in Rhodobacter capsulatus. Bba-bioenergetics, 2012; 1817 (6) : 898-910: http://dx.doi.org/10.1016/j.bbabio.2011.10.011
2011
Weiche, B., Bürk, J., Angelini, S., Schiltz, E., Thumfart, J. und Koch, H.-G. (2008). A cleavable N-terminal membrane anchor is involved in membrane binding of the Escherichia coli SRP receptor. J. Mol. Biol. 377, 761-773.
Peters, A., Kulajta, C., Pawlik, G., Daldal, F. und Koch, H.-G. (2008) Stability of cbb3 type cytochrome oxidase requires specific CcoQ-CcoP interactions. J. Bacteriol. 190, 5576-5586
Sanders, C., Turkarsalan, S., Onder, O., Frawley, E.R., Kranz, R.G., Koch, H.-G. und Daldal, F. (2008) Biogenesis of c-type cytochromes and cytochrome complexes. In: Hunter, C.N., Daldal, F., Thurnauer, M.C., und Beatty, J.T. (eds) The purple Phototrophic bacteria. Advances in Photosynthesis and Respiration Vol 28, pp. 407-423, Springer, Dordrecht, The Netherlands.
2010
Pawlik G, Kulajta C, Sachelaru I, Schroder S, Waidner B, Hellwig P, Daldal F, Koch HG: The putative assembly factor CcoH is stably associated with the cbb3-type cytochrome oxidase. J Bacteriol, 2010; 192 (24) : 6378-6389: http://dx.doi.org/10.1128/JB.00988-10
2009
Boy D, Koch HG: Visualization of distinct entities of the SecYEG translocon during translocation and integration of bacterial proteins. Mol Biol Cell, 2009; 20 (6) : 1804-1815: http://dx.doi.org/10.1091/mbc.E08-08-0886
Braig D, Bar C, Thumfart JO, Koch HG: Two cooperating helices constitute the lipid-binding domain of the bacterial SRP receptor. J Mol Biol, 2009; 390 (3) : 401-413: http://dx.doi.org/10.1016/j.jmb.2009.04.061
Burk J, Weiche B, Wenk M, Boy D, Nestel S, Heimrich B, Koch HG: Depletion of the signal recognition particle receptor inactivates ribosomes in Escherichia coli. J Bacteriol, 2009; 191 (22) : 7017-7026: http://dx.doi.org/10.1128/JB.00208-09
Mircheva M, Boy D, Weiche B, Hucke F, Graumann P, Koch HG: Predominant membrane localization is an essential feature of the bacterial signal recognition particle receptor. Bmc Biol, 2009; 7: 76-87: http://dx.doi.org/10.1186/1741-7007-7-76
2008
Weiche, B., Bürk, J., Angelini, S., Schiltz, E., Thumfart, J. und Koch, H.-G. (2008). A cleavable N-terminal membrane anchor is involved in membrane binding of the Escherichia coli SRP receptor. J. Mol. Biol. 377, 761-773.
Peters, A., Kulajta, C., Pawlik, G., Daldal, F. und Koch, H.-G. (2008) Stability of cbb3 type cytochrome oxidase requires specific CcoQ-CcoP interactions. J. Bacteriol. 190, 5576-5586
Sanders, C., Turkarsalan, S., Onder, O., Frawley, E.R., Kranz, R.G., Koch, H.-G. und Daldal, F. (2008) Biogenesis of c-type cytochromes and cytochrome complexes. In: Hunter, C.N., Daldal, F., Thurnauer, M.C., und Beatty, J.T. (eds) The purple Phototrophic bacteria. Advances in Photosynthesis and Respiration Vol 28, pp. 407-423, Springer, Dordrecht, The Netherlands.
2007
Koch, H.-G. und Schneider, D (2007) Folding, assembly and stability of transmembrane cytochromes. Current Chemical Biology 1, 59-74.
2006
Kulajta, C., Thumfart, J., Haid, S., Daldal, F. und Koch, H.-G. (2006). Multi-step assembly pathway of the cbb3-type cytochrome c oxidase complex. J. Mol. Biol. 355, 989-1004.
Aygun-Sunar, S., Mandaci, S., Koch, H.-G., Murray, I.V.J., Goldfine, H. und Daldal, F. (2006). Ornithine lipid is required for optimal steady-state amounts of c-type cytochromes in Rhodobacter capsulatus. Mol. Microbiol. 61, 418-435.
Angelini, S., Boy, D., Schiltz, E., und Koch, H.G. (2006). Membrane binding of the bacterial SRP receptor involves two distinct binding sites. J. Cell Biology 174, 715-724.
2005
Angelini, S., Deitermann, S., und Koch, H.-G. (2005). FtsY, the bacterial SRP receptor functionally and physically interacts with the SecYEG translocon. EMBO Reports 6, 476-481.
Deitermann, S., Sprie, G.S., und Koch, H.-G. (2005). A dual function for SecA in the assembly of single-spanning membrane proteins in Escherichia coli. J. Biol. Chem. 280, 39077-39085.
2004
Chevalier, N., Moser, M., Koch, H.-G., Schimz, K.-L., Willery, E., Locht, C., Müller, M. und Jacob-Dubuisson, F. (2004). Membrane targeting of a bacterial virulence factor harbouring an extended signal peptide. J. Mol. Microbiol. Biotechnol. 8, 7-18.
2003
Beha, D., Deitermann, S., Müller, M. und Koch, H.-G. (2003) Export of ß-lactamase is independent of the signal recognition particle (SRP). J. Biol. Chem. 278, 22161-22167.
Eisner, G., Koch, H.-G., Beck, K., Brunner, J. und Müller, M. (2003). Ligand Crowding at a Nascent Signal Sequence. J. Cell Biology 163, 35-44.
Alami, M., Lüke, I., Deitermann, S., Eisner, G., Koch, H.-G., Brunner, J. und Müller, M. (2003) Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli. Molecular Cell 12, 937-946.
Koch, H.-G., Moser, M. und Müller, M. (2003). Signal recognition particle (SRP)-dependent protein targeting, universal to all kingdoms of life. Rev. Physiol. Biochem. & Pharmacology 146, 55-94.
2002
Koch, H.-G., Moser, M., Schimz, K.-L. und Müller, M. (2002). The integration of YidC into the cytoplasmic membrane of E. coli requires the signal recognition particle, SecA and SecYEG. J. Biol. Chem. 277, 5715-5718.
2001
Swem, L., Elsen, S., Bird, T., Koch, H.-G., Myllykallio, H., Daldal, F. und Bauer, C.E. (2001). The RegB/RegA Two-component regulatory system controls synthesis of photosynthesis and respiratory electron transfer components in Rhodobacter capsulatus. J. Mol. Biol. 309, 121-138.
Müller, M., Koch, H.-G., Beck, K. und Schäfer, U. (2001). Protein traffic in eubacteria: Multiple routes from the ribosome to and across the membrane. Progress in Nucleic Acid Research and Molecular Biology 66, 107-157.
2000
Koch, H.-G., und Müller, M. (2000) Dissecting the translocase and integrase functions of the Escherichia coli SecYEG complex. J. Cell Biology 150, 689-694.
Koch, H.-G., Winterstein, C., Alben, J.O., A.S. Saribas und Daldal, F. (2000). Roles of the ccoGHIS gene products in the biogenesis of the cbb3-type cytochrome c oxidase. J. Mol. Biol. 297, 49-65.
Neumann-Haefelin, C., Schäfer, U., Müller, M. und Koch H.-G. (2000). SRP-dependent cotranslational targeting and SecA-dependent translocation analyzed as individual step in the export of a bacterial protein. EMBO J. 19, 6419-6426.
Beck, K., Koch, H.-G., Schäfer, U. und Müller, M. (2000). The SRP and SecA/SecB targeting pathways in E. coli exhibit distinct specificities in substrate recognition. In: Protein, Lipid and Membrane Traffic: Pathways and Targeting (Op den Kamp, J.A.F. Hrsg.), IOS Press, Amsterdam