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Identification of a putative alpha-glucan synthase essential for cell wall construction and morphogenesis in fission yeast.
Hochstenbach, F; Klis, F M; van den Ende, H; van Donselaar, E; Peters, P J; Klausner, R D.
Afiliación
  • Hochstenbach F; Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA. hochstenbach@bio.uva.nl
Proc Natl Acad Sci U S A ; 95(16): 9161-6, 1998 Aug 04.
Article en En | MEDLINE | ID: mdl-9689051
ABSTRACT
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.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Schizosaccharomyces / Pared Celular / Proteínas de Schizosaccharomyces pombe / Glucosiltransferasas Tipo de estudio: Diagnostic_studies / Prognostic_studies Idioma: En Revista: Proc Natl Acad Sci U S A Año: 1998 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Schizosaccharomyces / Pared Celular / Proteínas de Schizosaccharomyces pombe / Glucosiltransferasas Tipo de estudio: Diagnostic_studies / Prognostic_studies Idioma: En Revista: Proc Natl Acad Sci U S A Año: 1998 Tipo del documento: Article País de afiliación: Estados Unidos