First published online April 25, 2002; 10.1104/pp.010884
Plant Physiol, June 2002, Vol. 129, pp. 486-499
Prediction of Glycosylphosphatidylinositol-Anchored Proteins in
Arabidopsis. A Genomic Analysis1
Georg H.H.
Borner,
D. Janine
Sherrier,2
Timothy J.
Stevens,
Isaiah T.
Arkin,3 and
Paul
Dupree*
Department of Biochemistry, University of Cambridge, Cambridge, CB2
1QW, United Kingdom
Glycosylphosphatidylinositol (GPI) anchoring of proteins
provides a potential mechanism for targeting to the plant plasma membrane and cell wall. However, relatively few such proteins have been
identified. Here, we develop a procedure for database analysis to
identify GPI-anchored proteins (GAP) based on their possession of
common features. In a comprehensive search of the annotated Arabidopsis
genome, we identified 167 novel putative GAP in addition to the 43 previously described candidates. Many of these 210 proteins show
similarity to characterized cell surface proteins. The predicted GAP
include homologs of -1,3-glucanases (16), metallo- and aspartyl
proteases (13), glycerophosphodiesterases (6), phytocyanins (25),
multi-copper oxidases (2), extensins (6), plasma membrane receptors
(19), and lipid-transfer-proteins (18). Classical arabinogalactan (AG)
proteins (13), AG peptides (9), fasciclin-like proteins (20), COBRA and
10 homologs, and novel potential signaling peptides that we name GAPEPs
(8) were also identified. A further 34 proteins of unknown function
were predicted to be GPI anchored. A surprising finding was that over
40% of the proteins identified here have probable AG glycosylation
modules, suggesting that AG glycosylation of cell surface proteins is
widespread. This analysis shows that GPI anchoring is likely to be a
major modification in plants that is used to target a specific subset of proteins to the cell surface for extracellular matrix remodeling and signaling.
1
This work was supported by the
Biotechnology and Biological Sciences Research Council and by the
European Commission. G.H.H.B. also received a scholarship from the
Studienstiftung des Deutschen Volkes.
2
Present address: Department of Plant and Soil Sciences
and Delaware Biotechnology Institute, University of Delaware,
Newark, DE 19717.
3
Present address: Hebrew University Jerusalem, Department
of Biological Chemistry, Alexander Silberman Institute of Life
Sciences, Givat Ram, IL-91904 Jerusalem, Israel.
*
Corresponding author; e-mail p.dupree{at}bioc.cam.ac.uk; fax
44-1223-333345.
© 2002 American Society of Plant Physiologists
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