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.
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.
- 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)
- 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)
- 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
- 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
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,
Arabidopsis ABCG14 protein controls the acropetal translocation of root-synthesized
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.
acid 3-hydroxylase regulates Arabidopsis leaf longevity by mediating salicylic
Proc. Natl. Acad. Sci. USA, 110: 14807-14812 (2013)
X., Gou, M., and Liu, C.-J.
repeat F-box proteins regulate phenylpropanoid
biosynthesis via controlling the turnover of phenylalanine ammonia-lyase.
Plant Cell, 25: 4994-5010 (2013).
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
Mol. Plant, 6:1889-1903 (2013).
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
deacetylation of pectin impairs cell elongation, pollen germination, and
Plant Cell, 24: 50-65 (2012). PubMed
- Liu, C.-J.
Deciphering the enigma of lignification: Precursor transport,
oxidation, and the topochemistry of lignin
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
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
C.-J., Miao, Y.C. and Zhang, K.W.
Sequestration and transport of lignin monomeric precursors.
Molecules, 16: 710-727 (2011). PubMed
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).
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
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
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
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
A functional genomics investigation of allelochemical
biosynthesis in Sorghum biocolor root
J. Biol. Chem., 283: 3231-47 (2008). PubMed
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
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
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
Plant Mol. Biol., 62: 715-733 (2006). PubMed
H., Schröder, G., Wehinger,
E., Liu, C.-J., Noel, J.P., Schwab, W. and Schröder,
Methylation of sulfhydryl groups: a new function in a family of small
molecule plant O-methyltransferases.
Plant J., 46: 193-205 (2006). PubMed
C.-J., Deavours, B.E., Richard, S.B., Ferrer,
J.L., Blount, J.W., Huhman, D., Dixon, R.A. and
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
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).
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
C.-J., Huhman, D., Sumner, L.W. and Dixon, R.A.
Regiospecific hydroxylation of isoflavones by CYP81E enzymes in Medicago
Plant J., 36: 471-484 (2003). PubMed
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
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