Chang-Jun Liu

Brookhaven National Laboratory
Bldg. 463 - P.O. Box 5000
Upton, NY 11973-5000

Research Interests

Our research interests center on understanding the biosynthesis of phenylpropanoids in plants, the regulation of their biosynthetic pathways, and the structural modification of cell wall lignocelluloses.

Phenylpropanoids represent a large family of secondary metabolites in plants. Their biosynthesis in terrestrial species leads to the formation of a variety of phenolics and polyphenolics with diverse functions. They impart structural integrity to plants, e.g., cell-wall polymer lignin; they constitute biological barriers to control water- and solute-transportation, e.g., the (poly)aromatic domain of cell-wall suberin; and, as phytoalexins or signaling molecules, they modulate the plant’s defense responses and plant-environmental interactions, e.g., flavonoids, and isoflavonoids. These phenolic and polyphenolic metabolites in vascular plants constitute a major sink of organic carbon that, in some species, accounts for up to 30% photosynthetic carbon. The majority of them are deposited in cell walls, forming a complex aromatic polymer, viz., lignin. The cell-wall polysaccharides and lignin constitute the most abundant renewable biomass (lignocelluloses) on earth. However, the presence of intractable lignin in the cell-wall biomass is a formidable obstacle in producing renewable biofuels.

Through the integrated approaches of biochemistry, genomics/genetics, our group is undertaking four lines of research to resolve this stubborn problem. 1) Characterizing the biochemical functions and biological roles of the enzymes and proteins involved in the synthesis and modification, particularly O-acylation, of phenylpropanoids and cell-wall non-cellulosic polymers. 2) Exploring the molecular mechanisms of posttranslational regulation, and of the macromolecular organization of lignocelluloses’ biosynthetic enzymes. 3) Employing X-ray crystallographic strategies to study the structure-function of the key modification enzymes. 4) Utilizing the structural information on phenylpropanoid biosynthetic enzymes to design and create novel catalysts to modulate lignocellulosic structural properties. The goal of our studies is to obtain a deep understanding of the biosynthesis of phenylpropanoid, their structural modification, precursor transportation, and pathway regulation. We then will apply our knowledge to reduce the recalcitrance of lignocellulosic feedstock to degradation, and to enhance plant biomass production for efficient, sustainable biofuel production. Meanwhile, we anticipate engineering value-added chemicals for plant- and human- health, and for industrial applications.

Former group member:
Cheng Wang (Biotechnology and Bioengineering Center, Medical College of Wisconsin)

Selected Publications

• Bhuiya M.W. and Liu C.-J.
  A cost-effective colorimetric assay for phenolic O methyltransferases and characterization of caffeate 3-O-methyltransferases from Populus trichocarpa.
  Analytical Biochemistry, 384(1): 151-158 (January, 2009).  PubMed
• Yu, X.-H., Gou, J.-Y., and Liu C.-J.
  BAHD superfamily of acyl-CoA dependent acyltransferases in Populus and Arabidopsis: Bioinformatics and gene expression.
  Plant Mol Biol., 70(4):421-442 (July, 2009).  PubMed
• Baerson S.R., Dayan F.E., Rimando A.M., Dhammika Nanayakkara N.P., Liu C.J., Schroder J., Fishbein M., Pan Z., Kagan I.A., Pratt, L.H., Cordonnier-Pratt M.-M. and Duke S.O.
  A functional genomics investigation of allelochemical biosynthesis in Sorghum biocolor root hairs.
  J. Biol. Chem., 283(6):3231-47 (2008).  PubMed  
• Gou J., Park S., Yu X.-H., Miller L.M. and Liu C.-J.
  Compositional characterization and imaging of “wall-bound” acylesters of Populus trichocarpa reveal differential accumulation of acyl molecules in normal and reactive woods.
  Planta, 229(1):15-24 (December, 2008).   PubMed
• Yu X-H., Chen M.-H. and Liu C.-J.
  Nucleocytoplasmic-localized acyltransferases catalyze the malonylation of 7-O-glycosidic (iso)flavones in Medicago truncatula.
  Plant Journal, 55(3):382-396 (2008).  PubMed  
• Kao T., Liu C.-J., Yu X.-H., Young L., Connor D., Dilmanian A., Parham C., Reaney M. and Zhong, Z.
  Characterization of diffraction enhanced imaging contrast in plants.
  Nucl. Instru. Meth. Phys. Res. A, 582(1):208-211 (2007).
• Liu C.-J., Wang C., Noel J. P. and Dixon, R. A.
  Biochemical and structural bases for (iso)flavonoid biosynthetic diversity.
  In: Biotechnology and Sustainable Agriculture 2006 and Beyond (Z. Xu, J. Li, Y. Xue, and W. Yang, eds.), Springer-Verlag, The Netherlands, pp.231-234 (2007).
  
• Naoumkina M., Farag M.A., Sumner L.W., Tang Y., Liu C.-J. and Dixon, R.A.
  Different mechanisms for phytoalexin induction by pathogen and wound signals in Medicago truncatula.
  Proc. Natl. Acad. Sci. USA, 104(46):17909-17915 (2007). PubMed  
• Schulz R., Zhang Y.-B., Liu C.-J. and Freimuth P.
  Thiamine diphosphate binds to intermediates in the assembly of adenovirus fiber knob trimers in Escherichia coli.
  Protein Sci., 16(12):2684-2693 (2007). PubMed  
• Deavours B.E., Liu C.-J., Naoumkina M., Tang Y., Farag M.A., Sumner L.W., Noel J.P. and Dixon R.A.
  Functional analysis of members of the isoflavone and isoflavanone O-methyltransferase enzyme families from the model legume Medicago truncatula.
  Plant Mol Biol., 62(4-5):715-733 (2006).   PubMed  
• Coiner H., Schröder G., Wehinger E., Liu C.-J., Noel J.P., Schwab W. and Schröder J.
  Methylation of sulfhydryl groups: a new function in a family of small molecule plant O-methyltransferases.
  Plant J, 46(2):193-205 (2006).   PubMed  
• Liu C.-J., Deavours B.E., Richard S.B., Ferrer J.L., Blount J.W., Huhman D., Dixon R.A. and Noel J.P.
  Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses.
  Plant Cell, 18(12):3656-3669 (2006).   PubMed   Full Text
• Liu C.-J. and Noel J.P.
  Flavonoids: recent advances in molecular biology, biochemistry, pharmaceutical applications and metabolic engineering.
  In: Plant Genetic Engineering Vol. 7: Metabolic Engineering and Molecular Farming, (Ed. Jaiwal P.K.) Studium Press, Houston, pp 225-259 (2006).
• Yu X.-H. and Liu C.-J.
  Development of an analytical method for genome-wide functional identification of plant acyl-coenzyme A-dependent acyltransferases.
  Anal Biochem, 358(1):146-148 (2006).   PubMed  
• Liu C.-J., Huhman D., Sumner L.W. and Dixon R.A.
  Regiospecific hydroxylation of isoflavones by CYP81E enzymes in Medicago truncatula.
  Plant J., 36:471-484 (2003).   PubMed
• Dixon R.A., Achnine L., Kota P., Liu C.-J., Reddy M.K.S. and Wang L.
  The phenylpropanoid pathway and plant defense- a genomics perspective.
  Mol Plant Pathology, 3(5):371-390 (2002).   Abstract   Full Text
• Liu C.-J. and Dixon R.A.
  Directing metabolic flux toward engineered isoflavone nutraceuticals in transgenic Arabidopsis.
  In: Plant Biotechnology 2002 and Beyond, (Ed, Vasil I.K.), Kluwer Academic Publishers, pp 485-490 (2003).
• Liu C.-J., Blount J.W., Steele C.L. and Dixon R.A.
  Bottlenecks for the metabolic engineering of isoflavone glycoconjugates in Arabidopsis.
  Proc Natl Acad Sci USA, 99:14578-14583 (2002).  PubMed   Full Text
• Liu C.-J. and Dixon R.A.
  Elicitor-induced association of isoflavone O-methyltransferase with endomembranes prevents formation and 7-O-methylation of daidzein during isoflavonoid phytoalexin biosynthesis.
  Plant Cell, 13:2643-2658 (2001).   PubMed   Full Text
• Tan X.P., Liang W.Q., Liu C.-J., Luo P., Heinstein P. and Chen X.Y.
  Expression pattern of (+)-delta-cadinene synthase genes and biosynthesis of sesquiterpene aldehydes in plants of Gossypium arboreum L.
  Planta, 210(4):644-651 (2000).   PubMed
• Chen D.H., Liu C.-J., Ye H.C., Li G.F., Liu B.Y., Meng Y.L. and Chen X.Y.
  Ri-mediated transformation of Artemisia annua with a recombined farnesyl diphosphate synthase gene for artemisinin production.
  Plant Cell Tissue and Organ Culture 57, 157-162 (1999).
• Liu C.-J., Heinstein P. and Chen X.Y.
  Expression pattern of genes encoding farnesyl diphosphate synthase and sesquiterpene cyclase in cotton suspension-cultured cells treated with fungal elicitors.
  Mol Plant Microbe Interact, 12(12):1095-1104 (1999).   PubMed
• Liu C.-J. and Hou S.S.
  Regulation of saponin and polysaccharide biosynthesis in Panax ginseng suspended cells responding to the fungal elicitors.
  Acta Biologiae Experimentalis Sinica, 25:13-19 (1999).
• Meng Y.L., Jia J.W., Liu C.-J., Liang W.Q., Heinstein P. and Chen X.Y.
  Coordinated accumulation of (+)-delta-cadinene synthase mRNAs and gossypol in developing seeds of gossypium hirsutum and a new member of the cad1 family from G. arboreum.
  J Nat Prod., 62(2):248-252 (1999).   PubMed
• Liu C.-J., Meng Y.L., Hou S.S. and Chen X.Y.
  Cloning and sequencing of a cDNA encoding farnesyl pyrophosphate synthase from Gossypium arboreum and its expression pattern in developing cotton seeds of G. hirsutum c.v. Sumian-6.
  Acta Botanica Sinica, 24(8):703-710 (1998).

Last Modified: September 24, 2009
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