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Phenylcoumaran benzylic ether reductase, a prominent poplar xylem protein, is strongly associated with phenylpropanoid biosynthesis in lignifying cells

Kristine Vander Mijnsbrugge UGent, Hans Beeckman, Riet De Rycke UGent, Marc Van Montagu UGent, Gilbert Engler UGent and Wout Boerjan UGent (2000) PLANTA. 211(4). p.502-509
abstract
It has previously been shown (D.R. Gang et al., 1999, J Biol Chem 274: 7516-7527) that the most abundant protein in the secondary xylem of poplar (Populus trichocarpa cv. 'Trichobel') is a phenylcoumaran benzvlic ether reductase (PCBER), an enzyme involved in lignan synthesis. Here, the distribution and abundance of PCBER in poplar was studied at both the RNA and protein level. The cellular expression pattern was determined by immunolocalization of greenhouse-grown plants as well as of a field-grown poplar. Compared to other poplar tissues, PCBER is preferentially produced in the secondary xylem of stems and roots and is associated with the active growth period. The protein is present in all cells of the young differentiating xylem, corresponding to the zone of active phenylpropanoid metabolism and lignification. In addition. PCBER is located in young differentiating phloem fibers, in xylem ray parenchyma, and in xylem parenchyma cells at the growth-ring border. Essentially the same expression pattern was observed in poplars grown in greenhouses and in the field. The synthesis of PCBER in phenylpropanoid-synthesizing tissues was confirmed in a bending experiment. Induction of PCBER was observed in the pith of mechanically bent poplar stems, where phenylpropanoid metabolism is induced. These results indicate that the products of PCBER activity are synthesized mainly in lignifying tissues, suggesting a role in wood development.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
lignification, lignan, phenylcoumaran benzylic ether reductas, Populus (lignification), wood, xylem, CINNAMYL ALCOHOL-DEHYDROGENASE, PINORESINOL-LARICIRESINOL, PHYTOALEXIN BIOSYNTHESIS, ISOFLAVONE REDUCTASE, TRANSGENIC POPLAR, CDNA CLONING, EXPRESSION, PURIFICATION, DIVISION, PROMOTER
journal title
PLANTA
Planta
volume
211
issue
4
pages
502 - 509
Web of Science type
Article
Web of Science id
000089516200007
ISSN
0032-0935
DOI
10.1007/s004250000326
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
125039
handle
http://hdl.handle.net/1854/LU-125039
date created
2004-01-14 13:36:00
date last changed
2016-12-19 15:37:48
@article{125039,
  abstract     = {It has previously been shown (D.R. Gang et al., 1999, J Biol Chem 274: 7516-7527) that the most abundant protein in the secondary xylem of poplar (Populus trichocarpa cv. 'Trichobel') is a phenylcoumaran benzvlic ether reductase (PCBER), an enzyme involved in lignan synthesis. Here, the distribution and abundance of PCBER in poplar was studied at both the RNA and protein level. The cellular expression pattern was determined by immunolocalization of greenhouse-grown plants as well as of a field-grown poplar. Compared to other poplar tissues, PCBER is preferentially produced in the secondary xylem of stems and roots and is associated with the active growth period. The protein is present in all cells of the young differentiating xylem, corresponding to the zone of active phenylpropanoid metabolism and lignification. In addition. PCBER is located in young differentiating phloem fibers, in xylem ray parenchyma, and in xylem parenchyma cells at the growth-ring border. Essentially the same expression pattern was observed in poplars grown in greenhouses and in the field. The synthesis of PCBER in phenylpropanoid-synthesizing tissues was confirmed in a bending experiment. Induction of PCBER was observed in the pith of mechanically bent poplar stems, where phenylpropanoid metabolism is induced. These results indicate that the products of PCBER activity are synthesized mainly in lignifying tissues, suggesting a role in wood development.},
  author       = {Vander Mijnsbrugge, Kristine and Beeckman, Hans and De Rycke, Riet and Van Montagu, Marc and Engler, Gilbert and Boerjan, Wout},
  issn         = {0032-0935},
  journal      = {PLANTA},
  keyword      = {lignification,lignan,phenylcoumaran benzylic ether reductas,Populus (lignification),wood,xylem,CINNAMYL ALCOHOL-DEHYDROGENASE,PINORESINOL-LARICIRESINOL,PHYTOALEXIN BIOSYNTHESIS,ISOFLAVONE REDUCTASE,TRANSGENIC POPLAR,CDNA CLONING,EXPRESSION,PURIFICATION,DIVISION,PROMOTER},
  language     = {eng},
  number       = {4},
  pages        = {502--509},
  title        = {Phenylcoumaran benzylic ether reductase, a prominent poplar xylem protein, is strongly associated with phenylpropanoid biosynthesis in lignifying cells},
  url          = {http://dx.doi.org/10.1007/s004250000326},
  volume       = {211},
  year         = {2000},
}

Chicago
Vander Mijnsbrugge, Kristine, Hans Beeckman, Riet De Rycke, Marc Van Montagu, Gilbert Engler, and Wout Boerjan. 2000. “Phenylcoumaran Benzylic Ether Reductase, a Prominent Poplar Xylem Protein, Is Strongly Associated with Phenylpropanoid Biosynthesis in Lignifying Cells.” Planta 211 (4): 502–509.
APA
Vander Mijnsbrugge, K., Beeckman, H., De Rycke, R., Van Montagu, M., Engler, G., & Boerjan, W. (2000). Phenylcoumaran benzylic ether reductase, a prominent poplar xylem protein, is strongly associated with phenylpropanoid biosynthesis in lignifying cells. PLANTA, 211(4), 502–509.
Vancouver
1.
Vander Mijnsbrugge K, Beeckman H, De Rycke R, Van Montagu M, Engler G, Boerjan W. Phenylcoumaran benzylic ether reductase, a prominent poplar xylem protein, is strongly associated with phenylpropanoid biosynthesis in lignifying cells. PLANTA. 2000;211(4):502–9.
MLA
Vander Mijnsbrugge, Kristine, Hans Beeckman, Riet De Rycke, et al. “Phenylcoumaran Benzylic Ether Reductase, a Prominent Poplar Xylem Protein, Is Strongly Associated with Phenylpropanoid Biosynthesis in Lignifying Cells.” PLANTA 211.4 (2000): 502–509. Print.