The complex structures of arabinogalactan-proteins and the journey towards understanding function

被引:222
作者
Gaspar, Y
Johnson, KL
McKenna, JA
Bacic, A [1 ]
Schultz, CJ
机构
[1] Univ Melbourne, Plant Cell Biol Res Ctr, Parkville, Vic 3010, Australia
[2] Univ Melbourne, Cooperat Res Ctr Bioprod, Parkville, Vic 3010, Australia
基金
澳大利亚研究理事会;
关键词
Arabidopsis; arabinogalactan-protein; cell wall; fasciclin; glycosylphosphatidylinositol-anchor; hydroxyproline;
D O I
10.1023/A:1010683432529
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Arabinogalactan-proteins (AGPs) are a family of complex proteoglycans found in all higher plants. Although the precise function(s) of any single AGP is unknown, they are implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death. DNA sequencing projects have made possible the identification of the genes encoding a large number of putative AGP protein backbones. In contrast, our understanding of how AGPs undergo extensive post-translational modification is poor and it is important to understand these processes since they are likely to be critical for AGP function. Genes believed to be responsible for post-translational modification of an AGP protein backbone, include prolyl hydroxylases, glycosyl transferases, proteases and glycosylphosphatidylinositol-anchor synthesising enzymes. Here we examine models for proteoglycan function in animals and yeast to highlight possible strategies for determining the function(s) of individual AGPs in plants.
引用
收藏
页码:161 / 176
页数:16
相关论文
共 142 条
[1]  
Bacic A, 2000, CELL AND DEVELOPMENTAL BIOLOGY OF ARABINOGALACTAN-PROTEINS, P11
[2]   FINE-STRUCTURE OF THE ARABINOGALACTAN PROTEIN FROM LOLIUM-MULTIFLORUM [J].
BACIC, A ;
CHURMS, SC ;
STEPHEN, AM ;
COHEN, PB ;
FINCHER, GB .
CARBOHYDRATE RESEARCH, 1987, 162 (01) :85-93
[3]  
Bacic A., 1988, BIOCH PLANTS, P297, DOI DOI 10.1016/B978-0-08-092615-5.50014-X
[4]   Deletion of GPI7, a yeast gene required for addition of a side chain to the glycosylphosphatidylinositol (GPI) core structure, affects GPI protein transport, remodeling, and cell wall integrity [J].
Benachour, A ;
Sipos, G ;
Flury, I ;
Reggiori, F ;
Canivenc-Gansel, E ;
Vionnet, C ;
Conzelmann, A ;
Benghezal, M .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (21) :15251-15261
[5]   Yeast gpi8p is essential for GPI anchor attachment onto proteins [J].
Benghezal, M ;
Benachour, A ;
Rusconi, S ;
Aebi, M ;
Conzelmann, A .
EMBO JOURNAL, 1996, 15 (23) :6575-6583
[6]   Functional genomics in plants [J].
Bouchez, D ;
Höfte, H .
PLANT PHYSIOLOGY, 1998, 118 (03) :725-732
[7]  
Breton C, 1998, J BIOCHEM, V123, P1000
[8]   Virus-induced silencing of a plant cellulose synthase gene [J].
Burton, RA ;
Gibeaut, DM ;
Bacic, A ;
Findlay, K ;
Roberts, K ;
Hamilton, A ;
Baulcombe, DC ;
Fincher, GB .
PLANT CELL, 2000, 12 (05) :691-705
[9]  
BUTIKOFER P, 1993, J BIOL CHEM, V268, P17794
[10]   STRUCTURAL MODELS OF PRIMARY-CELL WALLS IN FLOWERING PLANTS - CONSISTENCY OF MOLECULAR-STRUCTURE WITH THE PHYSICAL-PROPERTIES OF THE WALLS DURING GROWTH [J].
CARPITA, NC ;
GIBEAUT, DM .
PLANT JOURNAL, 1993, 3 (01) :1-30