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Chang-Jun Liu

Principal Investigator

Background

Chang-Jun Liu earned his Ph.D. in 1999 at the Shanghai Institute of Plant Physiology, Graduate School, Chinese Academy of Science. In 2005, Chang-Jun Liu joined Brookhaven National Laboratory Biology Department working on research projects centered on phenylpropanoid biosynthesis, protein structure-function and engineering, cell wall lignocellulosic biogenesis and modification funded by DOE.

Phenylpropanoid Metabolism: Biosynthesis and Regulation

As the principal solar energy converter on Earth, plants effectively capture energy from sunlight and store it as reduced carbon through the process of photosynthesis. The fixed carbon is transported from source tissues to non-photosynthetic sink tissues, where it is allocated to the myriad of metabolic pathways including phenylpropanoid metabolism. Phenylpropanoid metabolism generates C6-C3 skeletons that are used to build a diverse array of phenolic compounds, including the methanolic soluble metabolites flavonoids/anthocyanins, stilbenes, coumarins and lignans, and the intractable cell wall polymer lignin. These phenolic metabolites possess diverse biological functions essential for plant growth and development, and plant- environmental interactions. In particular, as a structural component of plant secondary cell walls, lignin imparts strength, rigidity and water impermeability to plant vasculature, thus assuring the conductance of water and nutrients. Lignified secondary cell walls represent the most abundant bulk biomass of terrestrial plants. They are the renewable raw materials for pulping and paper making, and for producing bio-based chemicals and biofuels. However, on the other hand, the presence of lignin in cell wall impedes the enzymatic release of simple sugars from cell wall polysaccharides, thus lowering the fermentative production of cellulosic biofuels. Therefore, tailoring lignin biosynthesis is essential for the efficient utilization of cellulosic biomass resources. Since cell wall lignification is an irreversible biological process, it is under the tight control in respect to the carbon source allocation. A better understanding of the biochemical and regulatory mechanisms controlling carbon skeleton channeled into phenylpropanoid-lignin metabolism is critical for tailoring the biosynthetic activity for the purpose of producing renewable biofuels and bio-based products.

Research Interests

Our current research interests are primarily centered on the understanding of phenylpropanoid-lignin biosynthesis and the related regulatory mechanisms by which the plants employed to control the biosynthetic activity. We direct our researches to addressing the following questions: 1) How lignin and the related simple phenolics are synthesized and incorporated into cell walls; 2) how the synthesis, deposition and assembly processes are regulated at both transcriptional level and protein level; and 3) how lignification affects the structure and function of the cell walls. Ultimately we anticipate applying our knowledge gained from such fundamental studies to develop more effective strategies to manipulate lignification process, thereby lowering the recalcitrance of cell wall biomass for cost- effective production of biofuels and bio-based chemicals.

Through the integrated approaches of biochemistry, molecular genetics, structural biology, and protein engineering, we are specifically conducting the following research objectives: 1) Exploring the molecular mechanisms of post-translational regulation, and the macromolecular organization of phenylpropanoid-lignin biosynthesis; 2) Determining regulatory cascade or network controlling carbon allocation into phenylpropanoid metabolism; 3) Elucidating the structure-function relationship of the key enzymes in phenylpropanoid pathways, and engineer novel catalysts to modulate phenylpropanoid-lignin biosynthesis; 4) Characterizing the key enzymes and regulatory elements involved in the synthesis of "wall-bound" phenolics, including the phenolics incorporated into lipophilic polymer suberin and cutin; and 5) Metabolic engineering of phenylpropanoid biosynthesis to alter woody biomass digestive property or to produce high value chemicals.

Editorial Board

  • Scientific Reports (2016-present)
  • Frontiers in Plant Science, Plant Metabolism and Chemodiversity section (2015-present)
  • Acta of Plant Physiology (2015-present)

Membership and Committee

  • American Society of Plant Biologists
  • Phytochemical Society of North America
  • American Chemistry Society
  • International Collaborative Research and Renovation for Plant Metabolism, the Chinese Academy of Sciences (2009-2012)
  • Biochemistry and Structural Biology Graduate Program, Stony Brook University (2006-present)

Professional Awards

  • The Excellent Presidential Scholarship Award of the Chinese Academy of Sciences (1998)
  • The Director’s Award of Shanghai Institute of Plant Physiology (1998)
  • The Excellent Research Award, Shanghai-Beckman Life Science Foundation (1998)
  • The Excellent Scientific Researcher Award, Shanghai-Unilever (Britain) Developing Foundation (1998)
  • The Noble Foundation Postdoctoral Excellence Award (2003)

Patents

  • Liu, C.-J. and Bhuiya, M. W. (2014) Novel monolignol 4-O-methyltransferase uses and thereof (US patent No. 8889392)
  • Liu, C-J. and Cai, Y. (2013) Specialized (iso)eugenol-4-O-methyltransferases (s-IEMTs) and Methods of Making and Using the Same (US20140370568; application No US 14/306,511)

In the News

Selected Publications

  • Gou, M., Hou, G., Yang, H., Zhang, X., Cai, Y., Kai, G., and Liu, C.-J.
    The MYB107 transcription factor positively regulates suberin biosynthesis.
    Plant Physiol. 173: 1045–1058, DOI:10.1104/pp.16.01614 (2017)
  • Cai, Y., Zhang, K., Kim, H., Hou, G., Zhang, X., Yang, H., Feng, H., Miller, L., Ralph, J., and Liu, C.-J.
    Enhancing digestibility and ethanol yield of Populus wood via expression of an engineered monolignol 4-O-methyltransferase.
    Nature Communications 7: 11989 doi: 10.1038/ncomms11989 (2016)
  • Cai, Y., Bhuiya, M.-W., Shanklin, J., and Liu, C.-J.
    Engineering a monolignol 4-O-methyltransferase with high selectivity for the condensed lignin precursor coniferyl alchohol.
    J. Biol. Chem. 290: 26715-24. doi: 10.1074/jbc.M115.684217 (2015)
  • Zhang, X., Gou, M., Guo, C. R., Yang, H., and Liu, C.-J.
    Down-regulation of kelch domain-containing F-box protein in Arabidopsis enhances the production of (poly)phenols and tolerance to UV-radiation.
    Plant Physiol. 167: 337–350 (2015)
  • Zhang, X. and Liu, C.-J.
    Multifaceted regulations of gateway enzyme phenylalanine ammonia-lyase in the biosynthesis of phenylpropanoids.
    Mol. Plant 8: 17-27 (2015)
  • Liu, C.-J., Cai, Y.-H., Zhang, X., Gou, M., Yang, H.
    Tailoring lignin biosynthesis for efficient and sustainable biofuel production.
    Plant Biotech. J. 12: 1154-62 (2014)
  • Zhang, K., Novak, O., Wei, Z., Gou, M., Zhang, X., Yu, Y., Yang, H., Cai, Y., Strnad, M., and Liu, C.-J.
    Arabidopsis ABCG14 protein controls the acropetal translocation of root-synthesized cytokinins.
    Nature Communications, 5: 3274 (2014).
  • Xu, B., Gou, J.-Y., Li, F.G., Shangguan, X.X., Zhao, B., Yang, C.Q., Wang, L.J., Yuan, S., Liu, C.-J., and Chen X.Y.
    A cotton BURP domain protein interacts with α-expansin and their co-expression promotes plant growth and fruit production.
    Mol. Plant, 6: 945-958 (2013).
  • Zhang, K., Halitschke, R., Yin, C., Liu, C.-J., and Gan S.S.
    Salicylic acid 3-hydroxylase regulates Arabidopsis leaf longevity by mediating salicylic acid catabolism.
    Proc. Natl. Acad. Sci. USA, 110: 14807-14812 (2013)
  • Zhang, X., Gou, M., and Liu, C.-J.
    Arabidopsis kelch repeat F-box proteins regulate phenylpropanoid biosynthesis via controlling the turnover of phenylalanine ammonia-lyase.
    Plant Cell, 25: 4994-5010 (2013).
  • Cheng, A.X., Gou, J.Y., Yu, X.H., Yang, H., Fang, X., Chen, X.Y., and Liu, C.-J.
    Characterization and ectopic expression of a Populus hydroxyacid hydroxycinnamoyltransferase.
    Mol. Plant, 6:1889-1903 (2013).
  • Rimando, A.M., Pan, Z., Polashock, J.J., Dayan, F.E., Mizuno, C.S., Snook, M.E., Liu, C.-J., and Baerson S.R.
    In planta production of the highly potent resveratrol analogue pterostilbene via stilbene synthase and O-methyltransferase co-expression. Plant Biotech. J., 10: 269-283 (2012).
  • Zhang, K., Bhuiya, M.W., Pazo, J.R., Miao, Y., Kim, H., Ralph, J., and Liu, C.-J.
    An engineered monolignol 4-O-methyltransferase depresses lignin biosynthesis and confers novel metabolic capability in Arabidopsis.
    Plant Cell, 24:3135-3152 (2012).
  • Gou, J.Y., Miller, L.A., Hou, G., Yu, X.-H., Chen, X.-Y. and Liu, C.-J.
    Acetylesterase-mediated deacetylation of pectin impairs cell elongation, pollen germination, and plant reproduction.
    Plant Cell, 24: 50-65 (2012).   PubMed
  • Liu, C.-J.
    Deciphering the enigma of lignification: Precursor transport, oxidation, and the topochemistry of lignin assembly.
    Mol. Plant, 5: 304–317 (2012).  PubMed
  • Manjasetty, B.A., Yu, X.-H., Panjikar, S., Taguchi, G., Chance, M.R. and Liu, C.-J.
    Structural basis for modification of flavonol- and naphthol-glucoconjugates by Nicotiana tabacum malonyltransferase (NtMaT1).
    Planta, 236: 781–793 (2012).  PubMed
  • Gou, J.Y., Felippes, F.F., Liu, C.-J., Weigel, D. and Wang, J.W.
    Negative Regulation of Anthocyanin Biosynthesis in Arabidopsis by a miR156-Targeted SPL Transcription Factor.
    Plant Cell, 23: 1512-1522 (2011).   PubMed
  • Liu, C.-J., Miao, Y.C. and Zhang, K.W.
    Sequestration and transport of lignin monomeric precursors.
    Molecules, 16: 710-727 (2011).  PubMed
  • Bhuiya, M.W. and Liu, C.-J.
    Engineering monolignol 4-O-methyltransferases to modulate lignin biosynthesis.

    J. Biol. Chem., 285: 277-285 (2010).  PubMed
  • Liu, C.-J.
    Biosynthesis of hydroxycinnamate conjugates: Implications for sustainable biomass and biofuel production.
    Biofuels, 1: 745-761 (2010).
  • Miao, Y.-C. and Liu, C.-J.
    ATP-binding cassette-like transporters are involved in the transport of lignin precursors across plasma and vacuolar membranes.
    Proc. Natl. Acad. Sci. USA, 107: 22728-22733 (2010).  PubMed
  • 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.
    Anal. Biochem., 384: 151-158 (2009).  PubMed
  • Gou, J.-Y., Yu, X.-H. and Liu, C.-J.
    A hydroxycinnamoyltransferase responsible for synthesizing suberin aromatics in Arabidopsis.
    Proc. Natl. Acad. Sci. USA, 106: 18855-18860 (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: 421-442 (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: 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: 15-24 (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 J., 55: 382-396 (2008).  PubMed  
  • 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: 17909-17915 (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: 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: 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: 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: 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
  • 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., 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., 12:1095-1104 (1999).   PubMed