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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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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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MLA
Niculaes, Claudiu, et al. “Phenylcoumaran Benzylic Ether Reductase Prevents Accumulation of Compounds Formed under Oxidative Conditions in Poplar Xylem.” PLANT CELL, vol. 26, no. 9, 2014, pp. 3775–91, doi:10.1105/tpc.114.125260.
APA
Niculaes, C., Morreel, K., Kim, H., Lu, F., Mckee, L. S., Ivens, B., … Boerjan, W. (2014). Phenylcoumaran benzylic ether reductase prevents accumulation of compounds formed under oxidative conditions in poplar xylem. PLANT CELL, 26(9), 3775–3791. https://doi.org/10.1105/tpc.114.125260
Chicago author-date
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): 3775–91. https://doi.org/10.1105/tpc.114.125260.
Chicago author-date (all authors)
Niculaes, Claudiu, Kris Morreel, Hoon Kim, Fachuang Lu, Lauren S Mckee, Bart Ivens, Jurgen Haustraete, Bartel Vanholme, Riet De Rycke, Magnus Hertzberg, Jorg Fromm, Vincent Bulone, Andrea Polle, John Ralph, and Wout Boerjan. 2014. “Phenylcoumaran Benzylic Ether Reductase Prevents Accumulation of Compounds Formed under Oxidative Conditions in Poplar Xylem.” PLANT CELL 26 (9): 3775–3791. doi:10.1105/tpc.114.125260.
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.
IEEE
[1]
C. Niculaes et al., “Phenylcoumaran benzylic ether reductase prevents accumulation of compounds formed under oxidative conditions in poplar xylem,” PLANT CELL, vol. 26, no. 9, pp. 3775–3791, 2014.
@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}},
  keywords     = {{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://doi.org/10.1105/tpc.114.125260}},
  volume       = {{26}},
  year         = {{2014}},
}

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