Clint CS Chapple

Head/Distinguished Professor Biochem

Department: Biochemistry
Phone: 765.494.0494
Fax: 765.494.7897
Office: Head's Office: BCHM 120 / Research Office: WSLR B030
E-mail: chapple@purdue.edu

Area of Expertise: Biochemistry and molecular biology of plant secondary metabolism
Curriculum Vitae

Lignin, a major component of the cell wall of vascular plants, has long been recognized for its negative impact on forage quality, paper manufacturing, and more recently, cellulosic biofuel production. We focus on genetic and biochemical analysis of the well-known model Arabidopsis as well as the lycophyte Selaginella moellendorffii to advance our understanding of the relationship between ligninification and the utility of crops for bioenergy. Our work includes genetic engineering efforts aimed at generating energy crops with altered lignin, with the expectation that these strategies will similarly enhance forage digestibility and/or pulping efficiency. The knowledge gained from these bioengineering efforts has greatly improved our understanding of the optimal lignin characteristics required for different applications of lignocellulosic materials while also contributing to our understanding of the lignin biosynthetic pathway.

- Recent Publications

Weng, J. K., J. A. Banks, & C. C. Chapple (2010). Parallels in lignin biosynthesis: a study in Selaginella moellendorffii reveals convergence across 400 million years of evolution. Communicative and Intergrative Biology, 1(1), 1-3.

Schilmiller, A. L., J. Stout, J. K. Weng, J. Humphreys, M. O. Ruegger, & C. C. Chapple (2009). Mutations in the cinnamate 4-hydroxylase gene impact metabolism, growth and development in Arabidopsis. Plant Journal, 60, 771-782.

Weng, J. K., J. Stout, & C. Chapple (2008). Independent origins of syringyl lignin in vascular plants. The Proceedings of the National Academy of Sciences USA, 105(22), 7887-7892.

Stout, J., E. Romero-Severson, M. O. Ruegger, & C. C. Chapple (2008). Semi-dominant mutations in Reduced Epidermal Fluorescence 4 reduce phenylpropanoid content in Arabidopsis. Genetics, 178, 2237-2251.

Fraser, C. M., M. G. Thompson, A. M. Shirley, J. Ralph, J. A. Schoenherr, T. Siniapadech, M. C. Hall, & C. Chapple (2007). Related Arabidopsis serine carboxypeptidase-like sinapoylglucose acyltransferases display distinct but overlapping substrate specificities. Plant Physiology, 144, 1-14.

Sinlapadech, T., J. Stout, M. O. Ruegger, M. Deak, & C. C. Chapple (2007). The hyperfluorescent trichome phenotype of the brt1 mutant of Arabidopsis is the result of a defect in a gene encoding a sinapic acid: UDPG glucosyltransferase. Plant Journal, 49(4), 655-668.

Chapple, C. C., M. R. Hemm, S. D. Rider, & D. J. Murry (2004). Light induces phenylpropanoid metabolism in Arabidopsis roots. The Plant Journal, 38, 765-778.

Nair, R. B., K. L. Bastress, M. O. Ruegger, J. W. Denault, & C. C. Chapple (2004). The Arabidopsis REF1 gene encodes an aldehyde dehydrogenase involved in ferulic acid and sinapic acid biosynthesis. The Plant Cell, 16(16), 544-554.

Chapple, C. C., M. R. Hemm, & M. O. Ruegger (2003). The Arabidopsis ref2 mutant is defective in the gene encoding CYP83A1 and shows both phenylpropanoid and glucosinolate phenotypes. The Plant Cell, 15(1), 179-194.

Hemm, M. R., J. W. Deanult, M. O. Reugger, J. M. Humphreys, & C. C. Chapple (2002). Changes in secondary metabolism and deposition of an unusual lignin in the ref8 mutant of Arabidopsis. The Plant Journal, 30, 47-59.