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Research Paper |
Laboratoire de Génétique Moléculaire et Cellulaire, Institut National Agronomique Paris-Grignon, UMR-INRA216, URA-CNRS1925, BP01, 78850 Thiverval-Grignon, France1
Fungal Research Group, Swammerdam Institute for Life Sciences, University of Amsterdam, Nieuwe Achtergracht 166, 1018 WV Amsterdam, The Netherlands2
Aventis Pharma, 102 route de Noisy, 93235 Romainville cedex, France3
Laboratoire de Mycologie Fondamentale et Appliquée, INSERM EPI 9915, Université de Lille II, Faculté de Médecine H. Warembourg, Pôle Recherche, Place Verdun, 59037 Lille Cedex, France4
Author for correspondence: Mathias Richard. Tel: +33 1 30 81 54 53. Fax: +33 1 30 81 54 57. e-mail: richard{at}grignon.inra.fr
Glycosylphosphatidylinositol (GPI)-anchoring represents a mechanism for attaching proteins to the cell surface of all eukaryotic cells. Two localizations of GPI proteins have been observed in the yeasts Saccharomyces cerevisiae and Candida albicans: plasma membrane and cell wall. The signals and the mechanisms involved in this differential targeting are presently not well understood. Here several cell-wall-related phenotypes of a gpi7/las21 deletion are described, where GPI7/LAS21 encodes a GPI-anchor-modifying activity. In both organisms, the structure and composition of the cell wall was modified, with a clear increase in chitin deposition. Cell-wall-targeted proteins accumulated in the growth medium, whereas the protein content of the cell wall decreased significantly, suggesting inefficiency of the covalent linkage. The level of plasma-membrane-targeted GPI proteins was not affected. Sequence analyses revealed that gene families involved in the addition of phosphoethanolamines to the core GPI anchor are highly conserved between eukaryotes, with the exception of the Gpi7 family which seems to be fungus-specific. These data are compatible with the notion that the phosphoethanolamine added by Gpi7 protein to the GPI anchor is a key factor in the covalent linkage of cell-wall proteins to fungal cell-wall components.
Keywords: glycosylphosphatidylinositol, Pir proteins, Als proteins
Abbreviations: Als, agglutinin-like sequence; ConA, Concanavalin A; CWP, cell-wall protein; EtN, ethanolamine; EtN-P, phosphoethanolamine; GPI, glycosylphosphatidylinositol; Pir, protein with internal repeat
a Present address: Department of Microbiology, Columbia University, 701 West 168th Street, New York, NY 10032, USA.
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