Plant Physiology 76:414-417 (1984)
© 1984 American Society of Plant Biologists
Articles
Cross-Linking of Soluble Extensin in Isolated Cell Walls 1
James B. Cooper2 and
Joseph E. Varner
Plant Biology Program, Department of Biology, Washington University, St. Louis, Missouri 63130
The extensin component of primary cell walls has generally been considered to be an intrinsically insoluble cell wall glycoprotein. Recent data have established that cell wall extensin is in fact secreted in a soluble monomeric form which slowly becomes insolubilized in the cell wall probably through the oxidative formation of isodityrosine cross-links. We now show that isolated cell walls from aerated root slices of Daucus carota have the capacity to insolubilize extensin through the formation of isodityrosine. This in vitro cross-linking is specific for the extensin glycoprotein, as other wall proteins are not cross-linked by the isolated wall system. Although extensin can be cross-linked in solution by peroxidase and H2O2, dityrosine and not isodityrosine is the phenolic cross-link formed. Wall-catalyzed cross-linking of soluble extensin is inhibited by L-ascorbate, and both the initial rate and total extent of cross-linking are inhibited by acidic pH in the physiological range (pH 4 to 6). We suggest several mechanisms by which acid might inhibit cross-linking and propose that cytoplasmic factors (ascorbate and/or hydrogen ions) may regulate the solubility of extensin in vivo.
2 Present address: ARCO Plant Cell Research Institute, 6560 Trinity Ct., Dublin, CA 94568.
1 Supported by the National Science Foundation (PCM 8104516) and by a research contract from the Monsanto Company.
This article has been cited by other articles:
|
|
|
|
 
S. Gille, U. Hansel, M. Ziemann, and M. Pauly
Identification of plant cell wall mutants by means of a forward chemical genetic approach using hydrolases
PNAS,
August 25, 2009;
106(34):
14699 - 14704.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
J. Ribeiro, C. S. Pereira, N. Soares, A. Vieira, J. Feijo, and P. Jackson
The contribution of extensin network formation to rapid, hydrogen peroxide-mediated increases in grapevine callus wall resistance to fungal lytic enzymes
J. Exp. Bot.,
June 1, 2006;
57(9):
2025 - 2035.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
K. Roberts and A. H. Shirsat
Increased extensin levels in Arabidopsis affect inflorescence stem thickening and height
J. Exp. Bot.,
February 1, 2006;
57(3):
537 - 545.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
N. J. Price, C. Pinheiro, C. M. Soares, D. A. Ashford, C. P. Ricardo, and P. A. Jackson
A Biochemical and Molecular Characterization of LEP1, an Extensin Peroxidase from Lupin
J. Biol. Chem.,
October 17, 2003;
278(42):
41389 - 41399.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
P. A.P. Jackson, C. I.R. Galinha, C. S. Pereira, A. Fortunato, N. C. Soares, S. B.Q. Amancio, and C. P. P. Ricardo
Rapid Deposition of Extensin during the Elicitation of Grapevine Callus Cultures Is Specifically Catalyzed by a 40-Kilodalton Peroxidase
Plant Physiology,
November 1, 2001;
127(3):
1065 - 1076.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
U. Menke, N. Renault, and B. Mueller-Roeber
StGCPRP, a Potato Gene Strongly Expressed in Stomatal Guard Cells, Defines a Novel Type of Repetitive Proline-Rich Proteins
Plant Physiology,
March 1, 2000;
122(3):
677 - 686.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
T. J. Fowler, C. Bernhardt, and M. L. Tierney
Characterization and Expression of Four Proline-Rich Cell Wall Protein Genes in Arabidopsis Encoding Two Distinct Subsets of Multiple Domain Proteins
Plant Physiology,
December 1, 1999;
121(4):
1081 - 1091.
[Abstract]
[Full Text]
|
|
|
|
|
|
|
S. Morimoto, N. Tateishi, M. Inuyama, F. Taura, H. Tanaka, and Y. Shoyama
Identification and Molecular Characterization of Novel Peroxidase with Structural Protein-like Properties
J. Biol. Chem.,
September 10, 1999;
274(37):
26192 - 26198.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
