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Wood formation in poplar: identification, characterization, and seasonal variation of xylem proteins

Kristine Vander Mijnsbrugge UGent, Hugo Meyermans UGent, Marc Van Montagu UGent, Guy Bauw UGent and Wout Boerjan UGent (2000) PLANTA. 210(4). p.589-598
abstract
Proteins that are preferentially produced in developing xylem may play a substantial role in xylogenesis. To reveal the identity of these proteins, comparative two-dimensional polyacrylamide gel electrophoresis was performed on young differentiating xylem, mature xylem, and bark of poplar (Populus trichocarpa Hook. cv. 'Trichobel') harvested at different times of the year. The most-abundant xylem proteins were identified by microsequence analysis. For 17 of these proteins a putative function could be assigned based on similarity with previously characterized proteins, and for 15 out of these corresponding expressed sequence tags (ESTs) were found in the poplar EST database. The identified xylem-preferential proteins, defined by comparing the protein patterns from xylem and bark, were all involved in the phenylpropanoid pathway: two caffeoyl-coenzyme A O-methyltransferases (CCoAOMT), one phenylcoumaran benzylic ether reductase (PCBER), one bispecific caffeic acid/5-hydroxyferulic acid O-methyltransferase (COMT), five S-adenosyl-L-methionine synthetases, and one homologue of glycine hydroxymethyltransferase (GHMT). Remarkably, the biological function of the two most-abundant xylem-preferential proteins (PCBER and a GHMT homologue) remains unclear. In addition, several housekeeping enzymes were identified: two enolases, two glutamine synthetases, one 70-kDa heat-shock cognate, one calreticulin, and one alpha-tubulin. In comparison to the xylem-preferential proteins, the housekeeping proteins were expressed at significant levels in the bark as well. Also, several additional protein spots were detected for CCoAOMT, PCBER, and COMT by immunoblot. Our data show that for the study of xylogenesis, two-dimensional protein gel comparisons combined with systematic protein sequencing may yield information complementary to that from EST sequencing strategies.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
Populus, lignification, protein database, protein microsequencing, proteomics, wood formation, CAFFEOYL COENZYME-A, ISOFLAVONE REDUCTASE, CDNA CLONING, GENE-EXPRESSION, SERINE HYDROXYMETHYLTRANSFERASE, PHYTOALEXIN BIOSYNTHESIS, ARABIDOPSIS-THALIANA, GEL-ELECTROPHORESIS, MOLECULAR-GENETICS, SOLANUM-TUBEROSUM
journal title
PLANTA
Planta
volume
210
issue
4
pages
589 - 598
Web of Science type
Article
Web of Science id
000086458200009
ISSN
0032-0935
DOI
10.1007/s004250050048
language
English
UGent publication?
yes
classification
A1
additional info
the first two authors contributed equally to the work
copyright statement
I have transferred the copyright for this publication to the publisher
id
171066
handle
http://hdl.handle.net/1854/LU-171066
date created
2004-01-14 13:40:00
date last changed
2016-12-19 15:37:55
@article{171066,
  abstract     = {Proteins that are preferentially produced in developing xylem may play a substantial role in xylogenesis. To reveal the identity of these proteins, comparative two-dimensional polyacrylamide gel electrophoresis was performed on young differentiating xylem, mature xylem, and bark of poplar (Populus trichocarpa Hook. cv. 'Trichobel') harvested at different times of the year. The most-abundant xylem proteins were identified by microsequence analysis. For 17 of these proteins a putative function could be assigned based on similarity with previously characterized proteins, and for 15 out of these corresponding expressed sequence tags (ESTs) were found in the poplar EST database. The identified xylem-preferential proteins, defined by comparing the protein patterns from xylem and bark, were all involved in the phenylpropanoid pathway: two caffeoyl-coenzyme A O-methyltransferases (CCoAOMT), one phenylcoumaran benzylic ether reductase (PCBER), one bispecific caffeic acid/5-hydroxyferulic acid O-methyltransferase (COMT), five S-adenosyl-L-methionine synthetases, and one homologue of glycine hydroxymethyltransferase (GHMT). Remarkably, the biological function of the two most-abundant xylem-preferential proteins (PCBER and a GHMT homologue) remains unclear. In addition, several housekeeping enzymes were identified: two enolases, two glutamine synthetases, one 70-kDa heat-shock cognate, one calreticulin, and one alpha-tubulin. In comparison to the xylem-preferential proteins, the housekeeping proteins were expressed at significant levels in the bark as well. Also, several additional protein spots were detected for CCoAOMT, PCBER, and COMT by immunoblot. Our data show that for the study of xylogenesis, two-dimensional protein gel comparisons combined with systematic protein sequencing may yield information complementary to that from EST sequencing strategies.},
  author       = {Vander Mijnsbrugge, Kristine and Meyermans, Hugo and Van Montagu, Marc and Bauw, Guy and Boerjan, Wout},
  issn         = {0032-0935},
  journal      = {PLANTA},
  keyword      = {Populus,lignification,protein database,protein microsequencing,proteomics,wood formation,CAFFEOYL COENZYME-A,ISOFLAVONE REDUCTASE,CDNA CLONING,GENE-EXPRESSION,SERINE HYDROXYMETHYLTRANSFERASE,PHYTOALEXIN BIOSYNTHESIS,ARABIDOPSIS-THALIANA,GEL-ELECTROPHORESIS,MOLECULAR-GENETICS,SOLANUM-TUBEROSUM},
  language     = {eng},
  number       = {4},
  pages        = {589--598},
  title        = {Wood formation in poplar: identification, characterization, and seasonal variation of xylem proteins},
  url          = {http://dx.doi.org/10.1007/s004250050048},
  volume       = {210},
  year         = {2000},
}

Chicago
Vander Mijnsbrugge, Kristine, Hugo Meyermans, Marc Van Montagu, Guy Bauw, and Wout Boerjan. 2000. “Wood Formation in Poplar: Identification, Characterization, and Seasonal Variation of Xylem Proteins.” Planta 210 (4): 589–598.
APA
Vander Mijnsbrugge, K., Meyermans, H., Van Montagu, M., Bauw, G., & Boerjan, W. (2000). Wood formation in poplar: identification, characterization, and seasonal variation of xylem proteins. PLANTA, 210(4), 589–598.
Vancouver
1.
Vander Mijnsbrugge K, Meyermans H, Van Montagu M, Bauw G, Boerjan W. Wood formation in poplar: identification, characterization, and seasonal variation of xylem proteins. PLANTA. 2000;210(4):589–98.
MLA
Vander Mijnsbrugge, Kristine, Hugo Meyermans, Marc Van Montagu, et al. “Wood Formation in Poplar: Identification, Characterization, and Seasonal Variation of Xylem Proteins.” PLANTA 210.4 (2000): 589–598. Print.