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Professor of Microbiology

Nicole Frankenberg-Dinkel

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Curriculum vitae:

  • 1990-1996 Studies of Biology at the Universities of Regensburg, Germany and Boulder, Colorado, USA
  • 1996 Diploma thesis at the University of Regensburg; Supervisor: Günter Hauska
  • 1996-1999 PhD in Biochemistry at the University of Freiburg, Germany; Supervisor: Dieter Jahn
  • 1999-2002 Postdoc at the Department of Molecular and Cellular Biology, University of California at Davis, USA; Supervisor: J. Clark Lagarias
  • 2003-2005 Group leader within the Emmy-Noether-Program (DFG) at the Technical University Braunschweig, Germany
  • 2006-2014 W2-Professor for Physiology of Microorganisms at the Ruhr University Bochum, Germany
  • Since 09/2014 W3-Professor for Microbiology at the Technical University Kaiserslautern, Germany

Major Research Interest:

1.      Biosynthesis of light-harvesting pigments in cyanobacteria, cyanophages and unicellular algae (cryptophytes)

In addition to chlorophyll, cyanobacteria and certain type of algae use so-called phycobiliproteins to harvest light for photosynthesis. These phycobiliproteins employ colorful pigments belonging to the class of open-chain tetrapyrroles, which are covalently attached to the proteins. All these open-chain tetrapyrrole pigments are derived from one precursor molecule which is heme. After a ring opening reaction to give the first open-chain product biliverdin IXa, this molecule is further reduced by enzymes of the ferredoxin-dependent bilin reductases. We are employing recombinant enzymes to study the structure, function and evolution of these enzymes. Methods established in the lab include recombinant enzyme production and purification, UV/vis spectroscopy, HPLC, site-directed mutagenesis, X-ray crystallography (in cooperation) etc.


2.      Assembly of light-harvesting phycobiliproteins in cyanobacteria and unicellular algae (cryptophytes)

Once synthesized, the open-chain tetrapyrrole pigments have to be delivered and attached to the phycobiliprotein. This is done with the help of phycobiliprotein lyases, chaperon-like enzyme, which bind the pigment and deliver it to the right position of the phycobiliprotein. Within this project we study the structure, function and mechanism of pigment binding and delivery with similar methods as above.

3.       Sensorproteins in Bacteria and Archaea

Due to constantly changing environmental conditions, prokaryotes permanently have to adapt to their surroundings. Therefore, many sophisticated sensor proteins have been developed, which help the organisms to monitor their environment. Within this project we study various sensor proteins from Bacteria and Archaea, which are involved in sensing light (Pseudomonas aeruginosa phytochrome), redox state (the heme-based sensor MsmS from Methanosarcina acetivorans) and nitric oxid (the phosphodiesterase NbdA from P. aeruginosa and the H-NOX protein from Dinoroseobacter shibae). In all projects we investigate recombinant enzymes produced in E. coli and purified thereafter. Our main interest is to understand the molecular mechanisms by which the signals are perceived and transduced to a certain output module (histidine kinase, phosphodiesterase etc.).

4.     Molecular mechanisms of biofilm dispersal in Pseudomonas aeruginosa

Many bacterial species are able to form biofilms, large aggregates of cells which are embedded in a self-produced matrix. The life cycle of a biofilm does not only include its formation but also the dispersal. The latter occurs naturally but can also be triggered by certain environmental cues and is always connected to changes in the second messenger c-di-GMP. Using a combination of molecular genetics, phenotypic analyses and in vitro studies employing recombinant enzymes we are trying to understand the molecular details by which dispersion of Pseudomonas aeruginosa biofilms is initiated.

Selected Publications

  • Overkamp, K.E., Gasper, R., Kock, K., Herrmann, C., Hofmann, E. & Frankenberg-Dinkel, N. (2014) Insights into the Biosynthesis and Assembly of Cryptophycean Phycobiliproteins. J Biol. Chem. 289, 26691-26707.

  • Li, Y., Heine, S., Entian, M., Sauer, K. & Frankenberg-Dinkel, N. (2013) NO-induced biofilm dispersion in Pseudomonas aeruginosa is mediated by an MHYT-domain coupled phosphodiesterase. J. Bacteriol. 195, 3531-3542.

  • Molitor, B., Stassen, M., Modi, A., El-Mashtoly, S.F., Laurich, C., Lubitz, W., Dawson, J.H., Rother, M., & Frankenberg-Dinkel, N. (2013) A heme-based redox sensor in the methanogenic archaeon Methanosarcina acetivorans. J. Biol. Chem. 288, 18458-18472.

  • Busch, A.W.U., Reijerse, E.J., Lubitz, W., Frankenberg-Dinkel, N.* & Hofmann, E.* (2011) Structural and mechanistic insights into the ferredoxin-mediated two-electron reduction of bilins. Biochem. J. 439, 264-257.  *corresponding author

  • Dammeyer, T., Bagby, S.C., Sullivan, M. B., Chisholm, S. W. & Frankenberg-Dinkel, N. (2008) Efficient phage-mediated pigment biosynthesis in oceanic cyanobacteria. Curr. Biol.18, 442-448.