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J. Biol. Chem., Vol. 281, Issue 17, 11523-11529, April 28, 2006

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Pir Proteins of Saccharomyces cerevisiae Are Attached to -1,3-Glucan by a New Protein-Carbohydrate Linkage^*

Margit Ecker¹², Rainer Deutzmann¹, Ludwig Lehle¹, Vladimir Mrsa³, and Widmar Tanner⁴

From the Lehrstuhl für Zellbiologie und Pflanzenphysiologie, Universitaet Regensburg, Universitaetsstrasse 31, 93053 Regensburg, Germany and the Institut für Biochemie, Universitaet Regensburg, Universitaetsstrasse 31, 93053 Regensburg, Germany

A family of covalently linked cell wall proteins of Saccharomyces cerevisiae, called Pir proteins, are characterized by up to 10 conserved repeating units. Ccw5/Pir4p contains only one complete repeating sequence and its deletion caused a release of the protein into the medium. The exchange of each of three glutamines (Gln⁶⁹, Gln⁷⁴, Gln⁷⁶) as well as one aspartic acid (Asp⁷²) within the repeating unit leads to a loss of the protein from the cell wall. Amino acid sequencing revealed that only Gln⁷⁴ is modified. Release of the protein with mild alkali, changed Gln⁷⁴ to to glutamic acid, suggesting that Gln⁷⁴ is involved in the linkage. Analysis by mass spectrometry showed that 5 hexoses are attached to Gln/Glu⁷⁴. Sugar analysis revealed glucose as the only constituent. It is suggested that Pir proteins form novel, alkali labile ester linkages between the -carboxyl group of glutamic acids, arising from specific glutamines, with hydroxyl groups of glucoses of -1,3-glucan chains. This transglutaminase-type reaction could take place extracellularly and would energetically proceed on the account of amido group elimination.

Received for publication, January 12, 2006 , and in revised form, February 22, 2006.

^* This work was supported by the Deutsche Forschungsgemeinschaft (SFB 521) and by the Fonds der Chemischen Industrie. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ These authors have contributed equally to the results of this paper.

² Present address: Wilex AG, Grillparzerstr. 16, 81675 München, Germany.

³ Present address: Laboratory of Biochemistry, Faculty of Food Technology and Biotechnology, University of Zagreb, Pierottijeva 6, 10 000 Zagreb, Croatia.

⁴ To whom correspondence should be addressed. Tel.: 49-941-943-3018; Fax: 49-941-943-3352; E-mail: sekretariat.tanner{at}biologie.uni-regensburg.de.

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