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Prof. Dr. rer. nat. Thomas Brüser

Sprechzeiten:Do 10.00-12.00 Uhr

Zuordnung zu Einrichtungen:

  • Inst. f. Mikrobiologie
  • Naturwissenschaftliche Fakultät
  • Zentrum für Biomolekulare Wirkstoffe (BMWZ)


Prof. Thomas Brüser studied Biology (Biochemistry, Genetics, Organic Chemistry) at the University of Cologne and the University of Sussex (Brighton, UK) from 1989 to 1994.

1995-1999: PhD studies at the University of Bonn

1999: PhD in Microbiology: “Enzymology of oxidative sulfur metabolism: Biochemistry and genetics of bacterial APS:phosphate adenylyl transferases”

2000-2001: Postdoc at the University of Pennsylvania (Philadelphia, USA):  Cytochrome cbb3 biogenesis in Rhodobacter capsulatus and Tat-dependent protein translocation in Escherichia coli

2002-2009: Research group leader at the University of Halle-Wittenberg

2006: Habilitation in Microbiology: “Tat-dependent transport of proteins across biological membranes”

Since Oct. 2009: Full professor (W3) at the Leibniz University Hannover


2000: PhD award of the German Society of General and Applied Microbiology (VAAM)

2007: Christian-Wolff-Award of the University of Halle-Wittenberg

Research interests

  • Transport of folded proteins by the bacterial Tat pathway (more)
  • Membrane stress and the phage shock response (more
  • Periplasmic pyoverdine maturation and modification
  • Biofilm formation by plant growth-promoting rhizobacteria
  • Protein folding and cofactor assembly pathways 
  • Bacterial chaperone systems
  • Membrane protein complexes 
  • Microbial cell biology 
  • Anaerobic respirations 
  • Bacterial photosynthesis pathways





Geise, H., Heidrich, E.-S., Nikolin, C.S., Mehner-Breitfeld, D., and Brüser, T. (2019) A potential late stage intermediate of twin-arginine dependent protein translocation in Escherichia coli. Front. Microbiol., 10:1482


Mehner-Breitfeld, D., Rathmann, C., Riedel, T., Just, I., Gerhard, R., Overmann, J., and Brüser, T. (2018) Evidence for an adaptation of a phage-derived holin/endolysin system to toxin transport in Clostridioides difficile. Front. Microbiol., 9:2446


Ringel, M.T., and Brüser, T. (2018) The biosynthesis of pyoverdines. Microb. Cell, 5, 424-437


Heidrich, E.S., and Brüser, T. (2018) Evidence for a second regulatory binding site on PspF that is occupied by the C-terminal domain of PspA. PLoS ONE 13, e0198564


Hou, B., Heidrich, E.S., Mehner-Breitfeld, D., and Brüser, T. (2018) The TatA component of the twin-arginine translocation sysem locally weakens the cytoplasmic membrane of Escherichia coli upon protein substrate binding. J. Biol. Chem. 293, 7592-7605


Ringel, M.T., Dräger, G., and Brüser, T. (2018) PvdO is required for the oxidation of dihydropyoverdine as last step of fluorophore formation in Pseudomonas fluorescens. J. Biol. Chem. 293, 2330-2341


Ringel, M.T., Dräger, G., and Brüser, T. (2017) The periplasmic transaminase PtaA of Pseudomonas fluorescens converts the glutamic acid residue at the pyoverdine fluorophore to α-ketoglutaric acid. J. Biol. Chem. 292, 18660-18671


Thurotte, A., Brüser, T., Mascher, T. and Schneider, D. (2017) Membrane chaperoning by members of the PspA/IM30 protein family, Commun Integr Biol. 10, e1264546


Rathmann, C., Schlösser, A., Schiller, J., Bogdanov, M., and Brüser, T. (2017) Tat transport in Escherichia coli requires zwitterionic phosphatidylethanolamine but no specific negatively charged phospholipid. FEBS Lett. 591, 2848-2858


Ringel, M.T., Dräger, G., and Brüser, T. (2016) PvdN enzyme catalyzes a periplasmic pyoverdine modification. J. Biol. Chem. 291, 23929-23938


Stolle, P., Hou, B., and Brüser, T. (2016) The Tat substrate CueO is transported in an incomplete folding state. J. Biol. Chem. 291, 13520-13528


Osadnik H, Schöpfel M, Heidrich E, Mehner D, Lilie H, Parthier C, Risselada HJ, Grubmüller H, Stubbs MT, Brüser T. (2015) The PspF-binding domain PspA1-144 and the PspA·F complex - New insights into the coiled-coil dependent regulation of AAA+ proteins. Mol. Microbiol. 98, 743-759


Taubert, J., Hou, B., Risselada, H.J., Mehner, D., Lünsdorf, H., Grubmüller, H., and Brüser, T. (2015) TatBC-independent TatA/Tat substrate interactions
contribute to transport efficiency. PLoS ONE 10, e0119761


Taubert, J., and Brüser, T. (2014) Twin-arginine translocation-arresting protein regions contact TatA and TatB. Biol. Chem. 395, 827-836


Niggemann, J., Bozko, P., Bruns, N., Wodtke, A., Gieseler, M.T., Thomas, K., Jahns, C., Nimtz, M., Reupke, I., Brüser, T., Auling, G., Malek, N., Kalesse, M. (2014) Baceridin, a cyclic hexapeptide from an epiphytic Bacillus strain, inhibits the proteasome. Chembiochem. 15, 1021-1029


Behrendt J, Brüser T. (2014) The TatBC complex of the Tat protein translocase in Escherichia coli and its transition to the substrate-bound TatABC complex. Biochemistry 53, 2344-2354


Mehner, D., Osadnik, H., Lünsdorf, H., and Brüser, T. (2012) The Tat system for membrane translocation of folded proteins recruits the membrane-stabilizing Psp machinery in Escherichia coli. J. Biol. Chem. 287, 27834-27842


Brehmer, T., Kerth, A., Graubner, W., Malesevich, M., Hou, B., Brüser, T., and Blume, A. (2012) Negatively charged phospholipids trigger the interaction of a bacterial Tat substrate precursor with lipid monolayers. Langmuir  28, 3534-3541


Hou, B., and Brüser, T. (2011) The Tat-dependent protein translocation pathway. Biomol. Concepts 2, 507-523


Lindenstrauß, U., Matos, C., Graubner, W., Robinson, C., and Brüser, T. (2010) Malfolded recombinant Tat substrates are Tat-independently degraded in Escherichia coli. FEBS Lett. 584, 3644-3648


Lindenstrauß, U., and Brüser, T. (2009) Tat-transport of linker-containing proteins in Escherichia coli. FEMS Lett. 295, 135-140


Weininger, U., Haupt, C., Schweimer, K., Graubner, W., Kovermann, M., Brüser, T., Scholz, C., Schaarschmidt, P., Zoldak, G., Schmidt, F.X., and Balbach, J. (2009) NMR solution structure of SlyD from Escherichia coli: Spatial separation of prolyl isomerase and chaperone function. J. Mol. Biol. 387, 295-305


Standar, K., Mehner, D., Osadnik, H., Berthelmann, F., Hause, G., Lünsdorf, H., and Brüser, T. (2008) PspA can form large scaffolds in Escherichia coli. FEBS Lett. 582, 3585-3589


Berthelmann, F., Mehner, D., Richter, S., Lindenstrauß, U. Hause, G., Lünsdorf, H., and Brüser, T. (2008) Recombinant expression of tatABC and tatAC results in the formation of interacting cytoplasmic TatA-tubes in Escherichia coli. J. Biol. Chem. 283, 25281-25289


Natale, P., Brüser, T., and Driessen, A.J. (2008) Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane - distinct translocases and mechanisms. BBA Biomembranes 1778, 1735-1756


Richter, S., Lindenstrauß, U., Lücke, C., Bayliss, R., and Brüser, T. (2007) Functional Tat transport of unstructured, small, hydrophilic proteins. J. Biol. Chem. 282, 33257-33264


Behrendt, J., Lindenstrauß, U., and Brüser, T. (2007) TatC recruits TatB and prevents its multimerization in Escherichia coli. FEBS Lett. 581, 4085-4090


Brüser, T. (2007) The twin-arginine translocation system and its capability for protein secretion in biotechnological protein production. Appl. Microbiol. Biotechnol. 76, 35-45


Graubner, W., Schierhorn, A., and Brüser, T. (2007) DnaK plays a pivotal role in Tat targeting of CueO and functions beside SlyD as a general Tat signal binding chaperone. J. Biol. Chem. 282, 7116-7124


Lindenstrauss, U., and Brüser, T. (2006) Conservation and variation between Rhodobacter capsulatus and Escherichia coli Tat systems. J. Bacteriol. 188, 7807-7814


Sturm, A., Schierhorn, A., Lindenstrauss, U., Lilie, H., and Brüser, T. (2006) YcdB from Escherichia coli reveals a novel class of Tat-dependently translocated hemoproteins. J. Biol. Chem., 281, 13972-13978


Richter, S., and Brüser, T. (2005) Targeting of unfolded PhoA to the Tat translocon of Escherichia coli. J. Biol. Chem. 280, 42723-42730


Berthelmann, F., and Brüser, T. (2004) Localization of the Tat translocon components in Escherichia coli. FEBS Lett. 569, 82-88


Behrendt, J., Standar, K., Lindenstrauss, U., and Brüser, T. (2004) Topological studies on the twin-arginine translocase component TatC. FEMS Microbiol. Lett. 234, 303-308


Kipping, M., Lilie, H., Lindenstrauss, U., Andreesen, J.R., Griesinger, C., Carlomagno, T., and Brüser, T. (2003) Structural studies on a twin-arginine signal sequence. FEBS Lett. 550, 18-22


Brüser, T., Brune, D., Yano, T., and Daldal, F. (2003) Membrane targeting of a folded and cofactor containing protein. Eur. J. Biochem. 270, 1211-1221


Brüser, T., and Sanders, C. (2003) An alternative model of the twin-arginine translocation system, Microbiol. Res. 158, 7-17


Rose, R. W., Brüser, T., Kissinger, J.C., and Pohlschröder, M. (2002) Adaptation of protein secretion to extremely high salt conditions by extensive use of the twin arginine translocation pathway. Mol. Microbiol. 45, 943-950


Brüser, T., Selmer, T., and Dahl, C. (2000) "ADP sulfurylase" from Thiobacillus denitrificans is an adenylylsulfate:phosphate adenylyltransferase and belongs to a new family of nucleotidyltransferases. J. Biol. Chem. 275, 1691-1698


Brüser, T., Deutzmann, R., and Dahl, C. (1998) Evidence against the double-arginine motif as the only determinant for protein translocation by a novel Sec-independent pathway in Escherichia coli. FEMS Microbiol. Lett.164, 329-336


Reinartz, M., Tschäpe, J., Brüser, T., Trüper, H.G., and Dahl, C. (1998) Sulfide oxidation in the phototrophic sulfur bacterium Chromatium vinosum. Arch. Microbiol. 170, 59-68


Brüser, T., Trüper, H.G., and Dahl, C. (1997) Cloning and sequencing of the gene encoding the high potential iron-sulfur protein (HiPIP) from the purple sulfur bacterium Chromatium vinosum. Biochim. Biophys. Acta 1352, 18-22


Strange, R.W., Dodd, F.E., Abraham, Z.H.L., Grossmann, J.G., Brüser, T., Eady, R.R., Smith, B.E., and Hasnain, S.S. (1995) The substrate binding site in nitrite reductase and its similarity to Zn carbonic anhydrase. Nature Struct. Biol. 2, 287-292


Howes, B.D., Abraham, Z.H.L., Lowe, D.J., Brüser, T., Eady, R.R., and Smith, B.E. (1994) EPR and electron nuclear double resonance (ENDOR) studies show nitrite binding to type two copper centers of the dissimilatory nitrite reductase of Alcaligenes xylosoxidans (NCIMB 11015). Biochemistry 33, 3171-3177