David Wilson
Professor of Molecular Biology
David Wilson




Department of Molecular Biology & Genetics
458 Biotechnology Building
Cornell University
Ithaca, NY 14853-2703


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Department Profile


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.

Research Description

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.