607.255.5706
dbw3@cornell.edu
458 Biotechnology Building
Professor of Molecular Biology
Publications | Research | Faculty
Background:
David Wilson is a Professor of Biochemistry, Molecular and Cell Biology. He received his B.A. from Harvard in 1961, his Ph.D. in Biochemistry from Stanford Medical School in 1966, and did postdoctoral work at the Department of Biophysics at Johns Hopkins Medical School from 1966-67 before coming to Cornell as an Assistant Professor in 1967. He is a member of the American Society of Biological Chemists, the American Society of Microbiologists and the American Association for the Advancement of Science. He is a member of the Johns Hopkins Society of Scholars and is director of the Cornell Institute for Comparative and Environmental Toxicology. Professor Wilson teaches BioBM 633.
My laboratory studies the enzymology of plant cell wall degradation with a major focus on cellulases. Enzymes that degrade insoluble substrates have important differences from most enzymes whose substrates are small soluble molecules. In addition, cellulases are important industrial enzymes and have potential in the production of renewable, non-polluting fuels and chemicals. We are using a combination of genomics, protein engineering, and molecular biology in our research.
We have been studying the high G-C gram variable soil bacterium, Thermobifida fusca, a moderate thermophile, for more than 20 years, as it is a major microorganism degrading plant cell walls in heated plant wastes such as compost piles. Its genome sequence has just been finished by the Joint Genome Institute of the DOE (http://genome.jgi-psf.org/draft_microbes/thefu/thefu.home.html). We have cloned, expressed and characterized the activity of the expressed proteins of six cellulase genes, two xylanase genes, a xyloglucanase gene, a b-1,3 glucanase gene, a b-glucosidase gene, and a regulatory gene, CelR. Three-dimensional structures have been determined for the catalytic domains of three of the cellulases and the xyloglucanase, while structures for a cellulase and the b-1,3 glucanase are being determined. Extensive site directed mutagenesis studies have been carried out on one of the cellulases and such studies have started on two others. We are developing tools to construct gene knockouts in T. fusca. The work in my laboratory was summarized in a recent article (Wilson, D.B. Studies of Thermobifida fusca plant cell wall degrading enzymes. Chem. Rec. 4, 72-82 (2004).
I am a member of a team that received a USDA grant, which supported the sequencing of three rumen bacteria including Fibrobacter succinogenes, which is a cellulolytic anaerobe. The F. succinogenes genome sequence shows that it does not contain any known processive cellulase genes, unlike all other well-studied cellulolytic microorganisms. It is interesting that the aerobic bacterium, Cytophiga hutchinsonii, genome also lacks known processive cellulase genes. This suggests that these two organisms may use novel mechanisms for degrading cellulose, which we are trying to determine.
Hao, Z., Chen, S. and Wilson, D.B. Cadmium and manganese transport genes in bacteria. In Recent Advances in Marine Biotechnology, Vol. 8 (Fingerman, M. and Nagabhushanam, R., eds.). Science Publishers, Inc., Enfield, NH, pp. 171-187 (2003).
Andre, G., Kanchanawong, P., Palma, R., Cho, H., Deng, X., Irwin, D., Himmel, M.E., Wilson, D.B. and Brady, J.W. Computational and experimental studies of the catalytic mechanism of Thermobifida fusca cellulase Cel6A (E2). Protein Eng. 16, 125-134 (2003).
Chen, S., Vincent, S., Wilson, D.B. and Ganem, B. Mapping of chorismate mutase and prephenate dehydrogenase domains in the Escherichia coli T-protein. Eur. J. Biochem. 270, 757-763 (2003).
Stahl, C.H., Wilson, D.B. and Lei, X.G. Comparison of extracellular Escherichia coli AppA phytases expressed in Streptomyces lividans and Pichia pastoris. Biotech. Letters 25, 827-831 (2003).
Irwin, D., Leathers, T.D., Greene, R.V. and Wilson, D.B. Corn fiber hydrolysis by Thermobifida fusca extracellular enzymes. Appl. Microbiol. Biotechnol. 61, 352-358 (2003).
Irwin, D.C., Cheng, M., Xiang, B., Rose, J.K.C. and Wilson, D.B. Cloning, expression and characterization of a family-74 xyloglucanase from Thermobifida fusca. Eur. J. Biochem. 270, 3083-3091 (2003).
Schloss, P.D., Hay, A.G., Wilson, D.B. and Walker, L.P. Molecular assessment of inoculum efficacy and process reproducibility in composting using ARISA. Transactions of the ASAE 46, 919-927 (2003).
Zhang, S., Van Pelt, C.K. and Wilson, D.B. Quantitative determination of noncovalent binding interactions using automated nanoelectrospray mass spectrometry. Analytical Chem. 75, 3010-3018 (2003).
Jung, H., Wilson, D.B. and Walker, L.P. Binding of Thermobifida fusca CDCel5A, CDCel6B and CDCel48A to easily hydrolysable and recalcitrant cellulose fractions on BMCC. Enzyme & Microbial Tech. 31, 941-948 (2003).
Chen, S., Vincent, S., Wilson, D.B. and Ganem, B. Mapping of chorismate mutase and prephenate dehydrogenase domains in the Escherichia coli T-protein. Eur. J. Biochem. 270, 757-763 (2003).
Jung, H., Wilson, D.B. and Walker, L.P. Binding and reversibility of Thermobifida fusca Cel5A, Cel6B, and Cel48A and their respective catalytic domains to bacterial microcrystalline cellulose. Biotechnol. Bioeng. 84, 151-159 (2003).
Zhang, S., Wilson, D.B. and Ganem, B. An engineered chorismate mutase with allosteric regulation. Bioorg. Med. Chem. 11, 3109-3114 (2003).
Zagorski, N. and Wilson, D.B. Characterization and comparison of metal accumulation in two Escherichia coli strains expressing either CopA or MntA, heavy metal-transporting bacterial P-type adenosine triphosphatases. Appl. Biochem. Biotechnol. 117, 33-48 (2004).
Castellanos, M., Wilson, D.B., Shuler, M.L. A modular minimal cell model: purine and pyrimidine transport and metabolism. Proc. Natl. Acad. Sci. USA 101, 6681-6686 (2004).
Wilson, D.B. Studies of Thermobifida fusca plant cell wall degrading enzymes. Chem. Rec. 4, 72-82 (2004).
Posta, K., Beki, E., Wilson, D.B., Kukolya, J. and Hornok, L. Cloning, characterization and phylogenetic relationships of cel5B, a new endoglucanase encoding gene from Thermobifida fusca. J. Basic Microbiol. 44, 383 (2004).
Master, E.R., Rudsander, U.J., Zhou, W., Henriksson, H., Divne, C., Denman, S., Wilson, D.B. and Teeri, T.T. Recombinant expression and enzymatic characterization of PttCel9A, a KOR homologue from Populus tremula x tremuloides. Biochem. 43, 10080-10089 (2004).
Zhou, W., Irwin, D.C., Escovar-Kousen, J. and Wilson, D.B. Kinetic studies of Thermobifida fusca Cel9A active site mutant enzymes. Biochem. 43, 9655-9663 (2004).
Sanchez, M.M., Irwin, D.C., Pastor, F.I., Wilson, D.B. and Diaz, P. Synergistic activity of Paenibacillus sp. BP-23 cellobiohydrolase Cel48C in association with the contiguous endoglucanase Cel9B and with endo- or exo-acting glucanases from Thermobifida fusca. Biotech. Bioeng. 87, 161-169 (2004).
Kim, J.H., Irwin, D. and Wilson, D.B. Purification and characterization of Thermobifida fusca xylanase 10B. Can. J. Microbiol. 50, 835-43 (2004).
Schloss, P.D., Hay, A.G., Wilson, D.B., Gossett, J.M. and Walker, L.P. Quantifying bacterial population dynamics in compost using 16S rRNA gene probes. Appl. Microbiol. Biotech. 66, 457-463 (2005).
Larsson, A.M., Bergfors, T., Dultz, E., Irwin, D.C., Roos, A., Driguez, H., Wilson, D.B. and Jones, T.A. Crystal structure of Thermobifida fusca endoglucanase Cel6A in complex with substrate and inhibitor: the role of tyrosine Y73 in substrate ring distortion. Biochemistry 44, 12915-12922 (2005).
Wilson, D.B. Genetic engineering of bacteria and their potential for bioremediation. In Bioremediation of Aquatic and Terrestrial Ecosystems (Fingerman, M. and Nagabhushanam, R., eds.). Science Publishers, Enfield, NH, pp. 31-39 (2005).