Wolfgang Liebl

Institut für Mikrobiologie und Genetik
Georg-August-Universität
Grisebachstr.8
D-37077 Göttingen, Germany

Tel.: (+49)-551-393795
Fax. (+49)-551-394897
email. wliebl@gwdg.de

 

 


 

since 2003

Full Professor (Applied Microbiology), Georg-August-Universität, Göttingen

1997-2003

Associate Professor (Applied Microbiology), Georg-August-Universität, Göttingen

1997

Habilitation (Microbiology), Technische Universität München

1986-1988 

Postdoctoral Fellow, Massachusetts Institute of Technology, Cambridge, MA, USA

1986

Ph.D. (Dr. rer. nat.), Technische Universität München

1984

Diploma (Biology), Technische Universität München

 

Research Interests of the Group

One of the main interests of our group is the analysis of polysaccharide and oligosaccharide breakdown and utilization by microorganisms adapted to extreme habitats. In the last few years, we have focussed our work on xylan and starch degrading enzyme systems from hyperthermophiles, i. e. organisms that grow optimally at 80°C or higher. These organisms represent very deep branches within the prokaryotic lineages of the phylogenetic tree of organisms. We are interested in unusual glycosyl hydrolases and transferases from Thermotoga maritima, the model organism of hyperthermophilic bacteria. Current projects are aimed at the elucidation of the biochemical properties, the molecular structure and catalytic mechanism, the function(s) of non-catalytic domains, and the cellular localization of selected enzymes of T. maritima. Other projects in the field of extremophilic microorganisms deal with the enzymology and molecular biology of thermoalkaliphiles and thermoacidophiles. We are presently engaged in the analysis of the genome sequence and of selected enzymes of the extreme thermoacidophilic archaeon Picrophilus torridus.


Another group of bacteria studied in the laboratory are the Gram-positive bacteria with a high G+C content. We employ molecular biological techniques to study and modify physiological traits of amino acid-producing corynebacteria and micrococci.


Also, the group is interested in the characterization of genome (metagenome) structures of various microbial habitats (Prof. Dr. W. Streit, PD Dr. R. Daniel). DNA libraries are constructed from microbial consortia and biofilms in order to explore the genetic diversity of the different environments. Also, classical activity-based screens are used for the isolation of novel enzymes useful for biotechnology.

 

 


Picrophilus torridus


 

 

Selected publications:

Wassenberg, D., Liebl, W., and R. Jaenicke (2000) Maltose-binding protein from the hyperthermophilic bacterium Thermotoga maritima: Stability and binding properties. J. Mol. Biol., 295:279-288.

Meissner, K., Wassenberg, D., and W. Liebl (2000) The ‘thermostabilising domain’ of the modular xylanase XynA of the hyperthermophilic bacterium Thermotoga maritima represents a novel type of binding domain with affinity for soluble xylan and mixed-linkage beta -1,3/beta -1,4-glucan. Mol. Microbiol, 36:898-912.

Raasch, C., Streit, W., Schanzer, J., Bibel, M., Gosslar, U. and W. Liebl (2000) Thermotoga maritima AglA, an extremely thermostable NAD+-, Mn2+ -, and thiol-dependent alpha-glucosidase. Extremophiles 4:189-200.

Roujeinikova, A., Raasch, C., Burke, J., Baker, P. J., Liebl, W., and D. W. Rice (2001) The crystal structure of Thermotoga maritima maltosyltransferase and its implications for the molecular basis of the novel transfer specificity. J. Mol. Biol. 312:119-131.

Entcheva, P., Liebl, W., Johann, A., Hartsch, T., and W. Streit  (2001)  Direct cloning from enrichment cultures, a reliable strategy for isolation of complete operons and genes from microbial consortia. Appl. Environ. Microbiol. 67:89-99.

Sterner, R., and W. Liebl (2001) Thermophilic adaptation of proteins. Crit. Rev. Biochem. Mol. Biol. 36:39-106.

Roujeinikova, A., Raasch, C., Sedelnikova, S., Liebl, W., and D. W. Rice (2002) The crystal structure of Thermotoga maritima 4-alpha-glucanotransferase and its acarbose complex: implications for substrate specificity and catalysis. J. Mol. Biol. 321:149-162.

Liebl, W., Kloos, W. E., and W. Ludwig (2002) Plasmid-borne macrolide resistance in Micrococcus luteus. Microbiology 148:2479-2487.

Raasch, C., Armbrecht, M., Streit, W., Höcker, B., Sträter, N., and Liebl, W. (2002) Identification of residues important for NAD+-binding by the Thermotoga maritima alpha-glucosidase AglA, a member of glycoside hydrolase family 4. FEBS Lett. 517:267-271.

Raasch, C., Roujeinikova, A., Meissner, H., Rice, D. W., and Liebl, W. (2002) Biochemical Properties and Structural Features of the Thermostable Maltodextrin Transglycosidases from Thermotoga maritima. Biologia 57/Suppl.11:101-108.

Lodge, J. A., Maier, T., Liebl, W., Hoffmann, V., and Sträter, N. (2003) Crystal structure of Thermotoga maritima alpha-glucosidase AglA defines a new clan of NAD+-dependent glycosidases. J. Biol. Chem. 278:19151-19158.

Tzvetkov, M., Klopprogge, C., Zelder, O., and Liebl, W. (2003) Genetic dissection of trehalose biosynthesis in Corynebacterium glutamicum: inactivation of trehalose production leads to impaired growth and an altered cell wall lipid composition. Microbiology 149:1659-1673.

Veith, B., Zverlov, V. V., Lunina, N. A., Berezina, O. V., Raasch, C., Velikodvorskaya, G. A., and Liebl, W. (2003) Comparative analysis of the recombinant alpha-glucosidases from the Thermotoga neapolitana and Thermotoga maritima maltodextrin utilization gene clusters. Biocatal. Biotransform. 21:147-158.

Bertoldo, C., Armbrecht, M., Becker, F., Schäfer, T., Antranikian, G., and Liebl, W. (2004) Cloning, sequencing and characterization of thermoalkalistable pullulanase type I from Anaerobranca gottschalkii. Appl. Environ. Microbiol. 70:3407-3416.

O. Fütterer, A. Angelov, H. Liesegang, G. Gottschalk, C. Schleper, B. Schepers, C. Dock, G. Antranikian, W. Liebl (2004) Genome sequence of Picrophilus torridus and its implications for life around pH 0. Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096.

 

 

 

page last updated 11 Juni 2004; Email comments, questions to: wliebl@gwdg.de