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Published on April 25, 2002; 10.1104/pp.010884

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Received September 27, 2001
Returned for revision November 8, 2001
Accepted January 7, 2002

Prediction of Glycosylphosphatidylinositol-Anchored Proteins in Arabidopsis. A Genomic Analysis

Georg H.H. Borner , D. Janine Sherrier , Timothy J. Stevens , Isaiah T. Arkin , and Paul Dupree *

Department of Biochemistry, University of Cambridge, Cambridge, CB2 1QW, United Kingdom

* Corresponding author; email: p.dupree{at}bioc.cam.ac.uk.

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 ß-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.




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