JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Montijn, R. C.
Right arrow Articles by Klis, F. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Montijn, R. C.
Right arrow Articles by Klis, F. M.

Journal of Bacteriology, December 1999, p. 7414-7420, Vol. 181, No. 24
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Localization of Synthesis of beta 1,6-Glucan in Saccharomyces cerevisiae

Roy C. Montijn,1,dagger Edwin Vink,1 Wally H. Müller,2 Arie J. Verkleij,2 Herman Van Den Ende,1 Bernard Henrissat,3 and Frans M. Klis1,*

Swammerdam Institute of Life Science, University of Amsterdam, BioCentrum Amsterdam, Amsterdam 1098 SM,1 and Department of Molecular Cell Biology, University of Utrecht, 3584 CH Utrecht,2 The Netherlands, and Architecture et Fonction des Macromolécules Biologiques, CNRS-IFR1, 13402 Marseille cedex 20, France3

Received 28 June 1999/Accepted 27 September 1999

beta 1,6-Glucan is a key component of the yeast cell wall, interconnecting cell wall proteins, beta 1,3-glucan, and chitin. It has been postulated that the synthesis of beta 1,6-glucan begins in the endoplasmic reticulum with the formation of protein-bound primer structures and that these primer structures are extended in the Golgi complex by two putative glucosyltransferases that are functionally redundant, Kre6 and Skn1. This is followed by maturation steps at the cell surface and by coupling to other cell wall macromolecules. We have reinvestigated the role of Kre6 and Skn1 in the biogenesis of beta 1,6-glucan. Using hydrophobic cluster analysis, we found that Kre6 and Skn1 show significant similarities to family 16 glycoside hydrolases but not to nucleotide diphospho-sugar glycosyltransferases, indicating that they are glucosyl hydrolases or transglucosylases instead of genuine glucosyltransferases. Next, using immunogold labeling, we tried to visualize intracellular beta 1,6-glucan in cryofixed sec1-1 cells which had accumulated secretory vesicles at the restrictive temperature. No intracellular labeling was observed, but the cell surface was heavily labeled. Consistent with this, we could detect substantial amounts of beta 1,6-glucan in isolated plasma membrane-derived microsomes but not in post-Golgi secretory vesicles. Taken together, our data indicate that the synthesis of beta 1,6-glucan takes place largely at the cell surface. An alternative function for Kre6 and Skn1 is discussed.

* Corresponding author. Mailing address: Swammerdam Institute of Life Science, University of Amsterdam, BioCentrum Amsterdam, Kruislaan 318, Amsterdam 1098 SM, The Netherlands. Phone: 31-20-525 7834. Fax: 31-20-525 7934. E-mail: klis{at}bio.uva.nl.

dagger Present address: TNO Nutrition and Food Research Institute, 3700 AJ Zeist, The Netherlands.

Journal of Bacteriology, December 1999, p. 7414-7420, Vol. 181, No. 24
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 1999 by the American Society for Microbiology. All rights reserved.