Hochstenbach F, Klis FM, van den Ende H, van Donselaar E, Peters PJ, Klausner RD Identification of a putative alpha-glucan synthase essential for cell wall construction and morphogenesis in fission yeast Proceedings of the National Academy of Sciences of the USA95 (1998)
9161-9166
Journal NLM ID:7505876 WWW link:http://www.pnas.org/content/95/16/9161.abstract Publisher: National Academy of Sciences Correspondence: hochstenbachbio.uva.nl Institutions: Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA, Institute for Molecular Cell Biology, BioCentrum Amsterdam, University of Amsterdam, Kruislaan 318, 1098 SM Amsterdam, The Netherlands, Department of Cell Biology, Faculty of Medicine and Institute of Biomembranes, Utrecht University, 3584 CX Utrecht, The Netherlands
The cell wall protects fungi against lysis and determines their cell shape. Alpha-glucan is a major carbohydrate component of the fungal cell wall, but its function is unknown and its synthase has remained elusive. Here, we describe a fission yeast gene, ags1+, which encodes a putative alpha-glucan synthase. In contrast to the structure of other carbohydrate polymer synthases, the predicted Ags1 protein consists of two probable catalytic domains for alpha-glucan assembly, namely an intracellular domain for alpha-glucan synthesis and an extracellular domain speculated to cross-link or remodel alpha-glucan. In addition, the predicted Ags1 protein contains a multipass transmembrane domain that might contribute to transport of alpha-glucan across the membrane. Loss of Ags1p function in a temperature-sensitive mutant results in cell lysis, whereas mutant cells grown at the semipermissive temperature contain decreased levels of cell wall alpha-glucan and fail to maintain rod shapes, causing rounding of the cells. These findings demonstrate that alpha-glucan is essential for fission yeast morphogenesis.
Methods: electron microscopy, enzymatic digestion, cloning, sequence analysis Synthetic data: enzymatic Comments, role: alpha-glucan consists of straight-chain polymers, approximately 200 glucose moieties in length, linked by alpha-(1->3)-glucosidic bonds (and some 7% of alpha-(1->4)-glucosidic bonds)
Related record ID(s): 40541, 40798, 40799, 40800 NCBI Taxonomy refs (TaxIDs):4896 Reference(s) to other database(s): GTC:G84443CB Show glycosyltransferases
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