Laboratory No 201

Lab-Head            Dr. Rolf Daniel

                            Diploma (Biology), Georg-August University of Göttingen, 1991

                            Dr. rer. nat. (Microbiology), Georg-August University of Göttingen, 1994

                            Postdoc (Microbiology), Georg-August University of Göttingen, 1994 - 1995

                            Postdoc (Cell Biology, Yeast Genetics), University of California, Berkeley, 1995 -1996

                            Group leader at the Department of Microbiology and Genetics of the Georg-August University of Göttingen, since 6/1996

 

 

 

 

Current Members of the Lab No. 201 are:

 

Dr. Rolf Daniel                                 rdaniel@gwdg.de

Susanne Bowien                                susannebowien@hotmail.com

Frank Hoster                                     fhoster@gwdg.de

Anja Knietsch                                    akniets@gwdg.de

Baris S. Özyurt                                 ozyurt23@hotmail.com

Jessica E. Schmitz                             jschmit2@gwdg.de

Caroline Toeche-Mittler                  ctoeche@gwdg.de

Sebastian Schwartz                           nonotanono@yahoo.com

Tanja Waschkowitz                          

Claudia Wirth                                    cwirth@gwdg.de

 

 

 

 

Research topics of the lab are:

 

1) Molecular and biochemical characterization of genes and gene products involved in the anaerobic conversion of glycerol to 1,3-propanediol by Citrobacter freundii and Clostridium pasteurianum.

Microorganisms such as Citrobacter freundii or Clostridium pasteurianum are able to grow anaerobically on glycerol as sole carbon and energy source. Glycerol is converted by enteric bacteria to 1,3-propanediol (major product), ethanol, 2,3-butanediol, acetic and lactic acids. The fermentation pattern of clostridia is different in that they form butyric acid and butanol in addition. As outlined in Fig. 1 four key enzymes are responsible for glycerol breakdown: glycerol dehydrogenase (DhaD), dihydroxyacetone kinase (DhaK), coenzyme B12-dependent glycerol dehydratase (DhaB, DhaC, DhaE), and 1,3-propanediol dehydrogenase (DhaT). In our group, the key enzymes and the corresponding genes of C. freundii have been identified and characterized. They are encoded by the dha regulon, the expression of which is induced when dihydroxyacetone or glycerol is present. In the case of C. pasteurianum, we have encountered the genetic organization and the gene products of the reductive branch of glycerol fermentation, which leads to the formation of 1,3-propanediol (Fig. 1).

The coenzyme B12-dependent glycerol dehydratase is from special interest because its reaction proceeds via a radical mechanism and its activity is the limiting factor for the biotechnological production of 1,3-propanediol. Our current research is focused on the mechanism of the reactivation reaction of suicide-inactivated glycerol dehydratase and the identification of novel dehydratases.

 

 

 

Daniel R., Gottschalk G. (1992) Growth temperature-dependent activity of glycerol dehydratase in Escherichia coli expressing the Citrobacter freundii dha regulon. FEMS Microbiol. Lett. 100, 281-286.

DANIEL R., BOENIGK R., GOTTSCHALK G. (1995) Purification of 1,3-propanediol dehydrogenase from Citrobacter freundii and cloning, sequencing and overexpression of the corresponding gene in Escherichia coli. J. Bacteriol. 177, 2151-2156.

DANIEL R., STUERTZ K., GOTTSCHALK G. (1995) Biochemical and molecular characterization of the oxidative branch of glycerol utilization by Citrobacter freundii. J. Bacteriol.177, 4392-4401.

SEYFRIED M., DANIEL R., GOTTSCHALK G. (1996) Cloning, sequencing and overexpression of the genes encoding coenzyme B12-dependent glycerol dehydratase of Citrobacter freundii. J. Bacteriol. 178, 5793-5796.

LUERS F., SEYFRIED M., DANIEL R., GOTTSCHALK G. (1997) Glycerol conversion to 1,3-propanediol by Clostridium pasteurianum: cloning and expression of the gene encoding 1,3-propanediol dehydrogenase. FEMS Microbiol. Lett. 154, 337-345.

MACIS L., DANIEL R., GOTTSCHALK G. (1998) Properties and sequence of the coenzyme B12-dependent glycerol dehydratase. FEMS Microbiol. Lett. 164, 21-28.

Daniel R., BOBIK T. A., Gottschalk G. (1998) Biochemistry of coenzyme B12-dependent glycerol and diol dehydratases and organization of the encoding genes. FEMS Microbiol. Rev. 22, 553-566.

Seifert C, Bowien S, Gottschalk G, Daniel R. (2001) Identification and expression of the genes and purification and characterization of the gene products involved in reactivation of coenzyme B12-dependent glycerol dehydratase of Citrobacter freundii. European Journal of Biochemistry 268, 2369-2378.

 

 

2) Construction of environmental libraries (metagenomic libraries) and screening for acquired abilities of the resulting recombinant organisms.

Naturally occurring assemblages of microorganisms often encompass a bewildering array of physiological, metabolic, and genetic diversity. It has been estimated that to date less than 1 % of the world’s organisms can be cultured by using standard techniques. Therefore, our approach is to use the genetic diversity of the microorganisms in an environment to encounter new or improved genes and gene products for biotechnological purposes. Our approach for the identification of such genes and gene products is outlined in Fig. 2.

 

 

 

 

HENNE A., DANIEL R., SCHMITZ R. A., GOTTSCHALK G. (1999) Construction of environmental DNA libraries in Escherichia coli and screening for the presence of genes conferring utilization of 4-hydroxybutyrate. Appl. Environ. Microbiol. 65, 3901-3907.

HENNE A.,SCHMITZ R. A., BÖMEKE, M., GOTTSCHALK G., DANIEL, R. (2000) Screening of environmental DNA libraries for the presence of genes lipolytic activity on Escherichia coli. Appl. Environ. Microbiol. 66:3113-3116.

Majernik A., Gottschalk G., Daniel R. (2001) Screening of environmental DNA libraries for the presence of genes conferring Na+ (Li+)/H+ antiporter activity on Escherichia coli: characterization of the recovered genes and the corresponding gene products. J. Bacteriol. 183, 6645-6653.

Daniel, R. (2002) Construction of environmental libraries for functional screening of enzyme activity. In: Directed molecular evolution of proteins. K. Johnson, S. Brakmann (eds.), pp. 63-78. Wiley-VCH Verlag, Weinheim.

 

 

3) Cloning and sequencing of the metagenomes from the Wadden Sea and the river Leine

Molecular phylogenetic surveys of different habitats revealed the existence of may new microbial species and lineages undetected by classical microbiological approaches. In order to gain insights into genomes of uncharacterized microbial species, we have started to conduct metagenomic studies employing marine and freshwater sediments as starting materials (Fig. 3). We have used sediments of the Wadden Sea and the river Leine as model environments for our studies. Methods for the direct isolation of high-molecular weight DNA from both habitats have been developed and genomic fragments have been cloned into cosmid, plasmid, and BAC vectors. The resulting complex DNA libraries represent a substantial fraction of the metagenomes of these habitats. These libraries provide access to the genomic characterization of uncultivated microorganisms. In addition, the constructed libraries serve as a rich source for the sequence or activity based identification of novel genes encoding biotechnologically important enzymes and pathways for the production of bioactive agents .

 

4) Other publications

DANIEL R., WARNECKE F., POTEKHINA J. S., GOTTSCHALK G. (1999) Identification of the syntrophic partners in a coculture coupling anaerobic methanol oxidation to Fe(III) reduction. FEMS Microbiol. Lett. 180, 197-203.

Schmitz R. A., Daniel R., Deppenmeier U., Gottschalk G. (2001) The anaerobic way of life. In: The Prokaryotes. third edition, B. Balows, H. G. Trüper, M. Dworkin, W. Harder, K. H. Schleifer (eds.), Springer Verlag, New York.

Hoster F., Daniel R., Gottschalk G. (2001) Isolation of a new Thermoanaerobacterium thermosaccharolyticum strain (FH1) producing a thermostable dextranase. J. Gen. Appl. Microbiol. 47, 187-192.