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Journal of Bacteriology, October 1998, p. 5030-5037, Vol. 180, No. 19
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
New Potential Cell Wall Glucanases of
Saccharomyces cerevisiae and Their Involvement in
Mating
Corinna
Cappellaro,
Vladimir
Mrsa, and
Widmar
Tanner*
Lehrstuhl für Zellbiologie und
Pflanzenphysiologie, Universität Regensburg, 93040 Regensburg, Germany
Received 28 May 1998/Accepted 3 August 1998
Biotinylation of intact Saccharomyces cerevisiae cells
with a nonpermeant reagent (Sulfo-NHS-LC-Biotin) allowed the
identification of seven cell wall proteins that were released from
intact cells by dithiothreitol (DTT). By N-terminal sequencing,
three of these proteins were identified as the known proteins
-exoglucanase 1 (Exg1p),
-endoglucanase (Bgl2p), and
chitinase (Cts1p). One protein was related to the PIR protein family,
whereas the remaining three (Scw3p, Scw4p, and Scw10p [for soluble
cell wall proteins]) were found to be related to
glucanases. Single knockouts of these three potential glucanases
did not result in dramatic phenotypes. The double knockout of
SCW4 and the homologous gene SCW10 resulted in
slower growth, significantly increased release of proteins from
intact cells by DTT, and highly decreased mating efficiency when these
two genes were disrupted in both mating types. The synergistic behavior
of the disruption of SCW4 and SCW10 was
partly antagonized by the disruption of BGL2. The data
are discussed in terms of a possible counterplay of transglucosidase
and glucosidase activities.
*
Corresponding author. Mailing address: Lehrstuhl
für Zellbiologie und Pflanzenphysiologie, Universität
Regensburg, 93040 Regensburg, Germany. Phone: 49 941 943 3018. Fax: 49 941 943 3352. E-mail:
widmar.tanner{at}biologie.uni-regensburg.de.

Present address: Institut für molekulare Genetik, 37077 Göttingen, Germany.
Journal of Bacteriology, October 1998, p. 5030-5037, Vol. 180, No. 19
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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