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Phenylcoumaran benzylic ether reductase prevents accumulation of compounds formed under oxidative conditions in poplar xylem

(2014) PLANT CELL. 26(9). p.3775-3791
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Biotechnology for a sustainable economy (Bio-Economy)
Abstract
Phenylcoumaran benzylic ether reductase (PCBER) is one of the most abundant proteins in poplar (Populus spp) xylem, but its biological role has remained obscure. In this work, metabolite profiling of transgenic poplar trees downregulated in PCBER revealed both the in vivo substrate and product of PCBER. Based on mass spectrometry and NMR data, the substrate was identified as a hexosylated 8-5-coupling product between sinapyl alcohol and guaiacylglycerol, and the product was identified as its benzyl-reduced form. This activity was confirmed in vitro using a purified recombinant PCBER expressed in Escherichia coli. Assays performed on 20 synthetic substrate analogs revealed the enzyme specificity. In addition, the xylem of PCBER-downregulated trees accumulated over 2000-fold higher levels of cysteine adducts of monolignol dimers. These compounds could be generated in vitro by simple oxidative coupling assays involving monolignols and cysteine. Altogether, our data suggest that the function of PCBER is to reduce phenylpropanoid dimers in planta to form antioxidants that protect the plant against oxidative damage. In addition to describing the catalytic activity of one of the most abundant enzymes in wood, we provide experimental evidence for the antioxidant role of a phenylpropanoid coupling product in planta.
Keywords
LIGNIN, LIGNIFICATION, PHENOLIC-COMPOUNDS, ISOFLAVONE REDUCTASES, PINORESINOL-LARICIRESINOL, STRUCTURAL-CHARACTERIZATION, MASS-SPECTROMETRY, ZINNIA MESOPHYLL-CELLS, TRACHEARY ELEMENT DIFFERENTIATION, PULSED-FIELD GRADIENTS

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Citation

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Chicago
Niculaes, Claudiu, Kris Morreel, Hoon Kim, Fachuang Lu, Lauren S Mckee, Bart Ivens, Jurgen Haustraete, et al. 2014. “Phenylcoumaran Benzylic Ether Reductase Prevents Accumulation of Compounds Formed Under Oxidative Conditions in Poplar Xylem.” Plant Cell 26 (9): 3775–3791.
APA
Niculaes, C., Morreel, K., Kim, H., Lu, F., Mckee, L. S., Ivens, B., Haustraete, J., et al. (2014). Phenylcoumaran benzylic ether reductase prevents accumulation of compounds formed under oxidative conditions in poplar xylem. PLANT CELL, 26(9), 3775–3791.
Vancouver
1.
Niculaes C, Morreel K, Kim H, Lu F, Mckee LS, Ivens B, et al. Phenylcoumaran benzylic ether reductase prevents accumulation of compounds formed under oxidative conditions in poplar xylem. PLANT CELL. 2014;26(9):3775–91.
MLA
Niculaes, Claudiu, Kris Morreel, Hoon Kim, et al. “Phenylcoumaran Benzylic Ether Reductase Prevents Accumulation of Compounds Formed Under Oxidative Conditions in Poplar Xylem.” PLANT CELL 26.9 (2014): 3775–3791. Print.
@article{5798709,
  abstract     = {Phenylcoumaran benzylic ether reductase (PCBER) is one of the most abundant proteins in poplar (Populus spp) xylem, but its biological role has remained obscure. In this work, metabolite profiling of transgenic poplar trees downregulated in PCBER revealed both the in vivo substrate and product of PCBER. Based on mass spectrometry and NMR data, the substrate was identified as a hexosylated 8-5-coupling product between sinapyl alcohol and guaiacylglycerol, and the product was identified as its benzyl-reduced form. This activity was confirmed in vitro using a purified recombinant PCBER expressed in Escherichia coli. Assays performed on 20 synthetic substrate analogs revealed the enzyme specificity. In addition, the xylem of PCBER-downregulated trees accumulated over 2000-fold higher levels of cysteine adducts of monolignol dimers. These compounds could be generated in vitro by simple oxidative coupling assays involving monolignols and cysteine. Altogether, our data suggest that the function of PCBER is to reduce phenylpropanoid dimers in planta to form antioxidants that protect the plant against oxidative damage. In addition to describing the catalytic activity of one of the most abundant enzymes in wood, we provide experimental evidence for the antioxidant role of a phenylpropanoid coupling product in planta.},
  author       = {Niculaes, Claudiu and Morreel, Kris and Kim, Hoon and Lu, Fachuang and Mckee, Lauren S and Ivens, Bart and Haustraete, Jurgen and Vanholme, Bartel and De Rycke, Riet and Hertzberg, Magnus and Fromm, Jorg and Bulone, Vincent and Polle, Andrea and Ralph, John and Boerjan, Wout},
  issn         = {1040-4651},
  journal      = {PLANT CELL},
  keyword      = {LIGNIN,LIGNIFICATION,PHENOLIC-COMPOUNDS,ISOFLAVONE REDUCTASES,PINORESINOL-LARICIRESINOL,STRUCTURAL-CHARACTERIZATION,MASS-SPECTROMETRY,ZINNIA MESOPHYLL-CELLS,TRACHEARY ELEMENT DIFFERENTIATION,PULSED-FIELD GRADIENTS},
  language     = {eng},
  number       = {9},
  pages        = {3775--3791},
  title        = {Phenylcoumaran benzylic ether reductase prevents accumulation of compounds formed under oxidative conditions in poplar xylem},
  url          = {http://dx.doi.org/10.1105/tpc.114.125260},
  volume       = {26},
  year         = {2014},
}

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