458 Biotechnology Building
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.
Kostylev M, Moran-Mirabal JM, Walker LP, Wilson DB. Determination of the molecular statesof the processive endocellulase Thermobifida fusca Cel9A during crystalline cellulose depolymerization. Biotechnol Bioeng. 2011 Aug 11. doi: 10.1002/bit.23299. [Epub ahead of print]
Kostylev M, Wilson DB. Determination of the catalytic base in family 48 glycosyl hydrolases. Appl Environ Microbiol. 2011;77:6274-6.
Top EM, Wilson DB. Special issue of Current Opinion in Microbiology, focused on 'Ecology and Industrial Microbiology'. Curr Opin Microbiol. 2011;14:227-8.
Wilson DB. Microbial diversity of cellulose hydrolysis. Curr Opin Microbiol. 2011;14:259-63.
Moraïs S, Barak Y, Caspi J, Hadar Y, Lamed R, Shoham Y, Wilson DB, Bayer EA. Cellulase-xylanase synergy in designer cellulosomes for enhanced degradation of a complex cellulosic substrate. MBio. 2010;. pii: e00285-10.
Caspi J, Barak Y, Haimovitz R, Gilary H, Irwin DC, Lamed R, Wilson DB, Bayer EA. Thermobifida fusca exoglucanase Cel6B is incompatible with the cellulosomal mode in contrast to endoglucanase Cel6A. Syst Synth Biol. 2010;4:193-201.
Wilson DB. Demonstration of the importance for cellulose hydrolysis of CelS, the most abundant cellulosomal cellulase in Clostridium thermocellum.Proc Natl Acad Sci U S A. 2010 ;107:17855-6.
Moraïs S, Heyman A, Barak Y, Caspi J, Wilson DB, Lamed R, Shoseyov O, Bayer EA.
Vuong TV, Wilson DB. Glycoside hydrolases: Catalytic base/nucleophile diversity. Biotechnol Bioeng. 2010 ;107:195-205.
Moraïs S, Barak Y, Caspi J, Hadar Y, Lamed R, Shoham Y, Wilson DB, Bayer EA. Contribution of a xylan-binding module to the degradation of a complex cellulosic substrate by designer cellulosomes. Appl Environ Microbiol. 2010 ;76:3787-96.
Vuong TV, Wilson DB. Processivity, synergism, and substrate specificity of Thermobifida fusca Cel6B. Appl Environ Microbiol. 2009;75:6655-61.
Wilson DB. The first evidence that a single cellulase can be essential for cellulose degradation in a cellulolytic microorganism. Mol Microbiol. 2009 74:1287-8.
Caspi J, Barak Y, Haimovitz R, Irwin D, Lamed R, Wilson DB, Bayer EA. Effect of linker length and dockerin position on conversion of a Thermobifida fusca endoglucanase to the cellulosomal mode. Appl Environ Microbiol. 2009;75:7335-42.
Vuong TV and Wilson, DB. The absence of a single identifiable catalytic base residue in Thermobifida fusca exocellulase Cel6B. FEBS J. 2009 ;276:3837-45.
McGrath CE, Vuong TV, Wilson DB. Site-directed mutagenesis to probe catalysis by a Thermobifida fusca beta-1,3-glucanase (Lam81A). Protein Eng Des Sel. 2009 22:375-82.
Wilson DB. Cellulases and biofuels. Curr Opin Biotechnol. 2009 20:295-9.
Wilson DB. Cellulases. Chapter in Encyclopedia of Microbiology 3d Edition. M. Schaechter Ed. Elsever Inc, San Diego 2009.
Echtenkamp PL, Wilson DB, Shuler ML. Cell cycle progression in Escherichia coli B/r affects transcription of certain genes: Implications for synthetic genome design. Biotechnol Bioeng. 2009 ;102:902-9.
Caspi J, Irwin D, Lamed R, Li Y, Fierobe HP, Wilson DB, Bayer EA. Conversion of Thermobifida fusca free exoglucanases into cellulosomal components: comparative impact on cellulose-degrading activity. J Biotechnol. 2008 ;135:351-7.
Moser F, Irwin D, Chen S, Wilson DB. Regulation and characterization of Thermobifida fusca carbohydrate-binding module proteins E7 and E8.Biotechnol Bioeng. 2008 ;100:1066-77.
McGrath,C.E. And Wilson,D.B. Endocellulytic activity of Clostridium thermocellum Cel9C (formerly CBHA) catalytic domain. Indust. Biotech. 2008 :4.99-104.
Wilson DB. Three microbial strategies for plant cell wall degradation. Ann N Y Acad Sci 2008;1125:289-97.
Li Y, Wilson DB. Chitin binding by Thermobifida fusca cellulase catalytic domains. Biotechnol Bioeng. 2008 Jul 1;100:644-52.
Rudsander UJ, Sandstrom C, Piens K, Master ER, Wilson DB, Brumer Iii H, Kenne L, Teeri TT. Comparative NMR analysis of cellooligosaccharide hydrolysis by GH9 bacterial and plant endo 1,4-beta-glucanases. Biochemistry. 2008;47(18):5235-41.
Wilson,D.B.Aerobic Microbial Cellulase Systems. Chapter 11 in Himmel, M. E., ed. Biomass Recalcitrance: Deconstructing the Plant Cell Wall for Bioenergy. Oxford, UK: Blackwell Publishing pp. 374-392.