Phenylcoumaran Benzylic Ether Reductase Prevents Accumulation of Compounds Formed under Oxidative Conditions in Poplar Xylem. Issue 9 (19th September 2014)
- Record Type:
- Journal Article
- Title:
- Phenylcoumaran Benzylic Ether Reductase Prevents Accumulation of Compounds Formed under Oxidative Conditions in Poplar Xylem. Issue 9 (19th September 2014)
- Main Title:
- Phenylcoumaran Benzylic Ether Reductase Prevents Accumulation of Compounds Formed under Oxidative Conditions in Poplar Xylem
- Authors:
- Niculaes, Claudiu
Morreel, Kris
Kim, Hoon
Lu, Fachuang
McKee, Lauren S.
Ivens, Bart
Haustraete, Jurgen
Vanholme, Bartel
Rycke, Riet De
Hertzberg, Magnus
Fromm, Jorg
Bulone, Vincent
Polle, Andrea
Ralph, John
Boerjan, Wout - Abstract:
- Abstract : This work reveals the biological function of phenylcoumaran benzylic ether reductase, one of the most abundant proteins in poplar wood. Its role is to reduce monolignol coupling products and to prevent accumulation of compounds formed under oxidative conditions. 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 enzymesAbstract : This work reveals the biological function of phenylcoumaran benzylic ether reductase, one of the most abundant proteins in poplar wood. Its role is to reduce monolignol coupling products and to prevent accumulation of compounds formed under oxidative conditions. 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. … (more)
- Is Part Of:
- The Plant Cell. Volume 26:Issue 9(2014)
- Journal:
- The Plant Cell
- Issue:
- Volume 26:Issue 9(2014)
- Issue Display:
- Volume 26, Issue 9 (2014)
- Year:
- 2014
- Volume:
- 26
- Issue:
- 9
- Issue Sort Value:
- 2014-0026-0009-0000
- Page Start:
- 3775
- Page End:
- 3791
- Publication Date:
- 2014-09-19
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.114.125260 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16316.xml