Plant Physiology 59:894-900 (1977)
© 1977 American Society of Plant Biologists
Articles
Relationships between Hydroxyproline-containing Proteins Secreted into the Cell Wall and Medium by Suspension-cultured Acer pseudoplatanus Cells 1
David G. Pope
a MSU/ERDA Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824
The pathway of hydroxyproline-containing proteins to the cell wall, and to the growth medium in suspension-cultured Acer pseudoplatanus cells is traced by following the kinetics of the transfer of protein-bound 14C-hydroxyproline into various fractions, and by comparing the hydroxyproline-arabinoside profiles of these fractions after alkaline hydrolysis.
Hydroxyproline-rich protein passes directly from a membrane-bound compartment in the cytoplasm to the cell wall, not via an intermediate salt-soluble pool in the wall.
There are at least three hydroxyproline-containing glycoproteins in the cell wall. One which possesses mono, tri, and tetraarabinoside side chains accounts for over 90% of the total hydroxyproline. This glycoprotein is "extensin."
The hydroxyproline-containing proteins secreted into the medium have a glycosylation pattern markedly different from that of the major cell wall glycoprotein. It appears that there is little or no wall-like extensin in the medium.
Approximately half of the protein-bound hydroxyproline secreted into the medium is linked to an arabinogalactan. This linkage is also found in a particulate wall protein precursor fraction from the cytoplasm, but only trace amounts can be detected in the cell wall.
1 This work was supported by United States Atomic Energy Commission Contract AT(11-1)-1338).
This article has been cited by other articles:

|
 |

|
 |
 
H. S. Sardar, J. Yang, and A. M. Showalter
Molecular Interactions of Arabinogalactan Proteins with Cortical Microtubules and F-Actin in Bright Yellow-2 Tobacco Cultured Cells
Plant Physiology,
December 1, 2006;
142(4):
1469 - 1479.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
J. M. Estevez, M. J. Kieliszewski, N. Khitrov, and C. Somerville
Characterization of Synthetic Hydroxyproline-Rich Proteoglycans with Arabinogalactan Protein and Extensin Motifs in Arabidopsis
Plant Physiology,
October 1, 2006;
142(2):
458 - 470.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
A. S. Karnoup, V. Turkelson, and W.H. K. Anderson
O-Linked glycosylation in maize-expressed human IgA1
Glycobiology,
October 1, 2005;
15(10):
965 - 981.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
L. Tan, F. Qiu, D. T. A. Lamport, and M. J. Kieliszewski
Structure of a Hydroxyproline (Hyp)-Arabinogalactan Polysaccharide from Repetitive Ala-Hyp Expressed in Transgenic Nicotiana tabacum
J. Biol. Chem.,
March 26, 2004;
279(13):
13156 - 13165.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
L. Tan, J. F. Leykam, and M. J. Kieliszewski
Glycosylation Motifs That Direct Arabinogalactan Addition to Arabinogalactan-Proteins
Plant Physiology,
July 1, 2003;
132(3):
1362 - 1369.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
E. Shpak, J. F. Leykam, and M. J. Kieliszewski
Synthetic genes for glycoprotein design and the elucidation of hydroxyproline-O-glycosylation codes
PNAS,
December 21, 1999;
96(26):
14736 - 14741.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
M. J. Kieliszewski, M. O'Neill, J. Leykam, and R. Orlando
Tandem Mass Spectrometry and Structural Elucidation of Glycopeptides from a Hydroxyproline-rich Plant Cell Wall Glycoprotein Indicate That Contiguous Hydroxyproline Residues Are the Major Sites of Hydroxyproline O-Arabinosylation
J. Biol. Chem.,
February 10, 1995;
270(6):
2541 - 2549.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
N. CARPITA, D. SABULARSE, D. MONTEZINOS, and D. P. DELMER
Determination of the Pore Size of Cell Walls of Living Plant Cells
Science,
September 14, 1979;
205(4411):
1144 - 1147.
[Abstract]
[PDF]
|
 |
|
|
|