Role of the synthase domain of Ags1p in cell wall alfa-glucan biosynthesis in fission yeast

A. Vos, N. Dekker, B. Distel, J.A.M. Leunissen, F. Hochstenbach

Research output: Contribution to journalArticleAcademicpeer-review

17 Citations (Scopus)

Abstract

The cell wall is important for maintenance of the structural integrity and morphology of fungal cells. Besides -glucan and chitin, -glucan is a major polysaccharide in the cell wall of many fungi. In the fission yeast Schizosaccharomyces pombe, cell wall -glucan is an essential component, consisting mainly of (1,3)--glucan with 10% (1,4)-linked -glucose residues. The multidomain protein Ags1p is required for -glucan biosynthesis and is conserved among cell wall -glucan-containing fungi. One of its domains shares amino acid sequence motifs with (1,4)--glucan synthases such as bacterial glycogen synthases and plant starch synthases. Whether Ags1p is involved in the synthesis of the (1,4)--glucan constituent of cell wall -glucan had remained unclear. Here, we show that overexpression of Ags1p in S. pombe cells results in accumulation of (1,4)--glucan. To determine whether the synthase domain of Ags1p is responsible for this activity, we overexpressed Ags1p-E1526A, which carries a mutation in a putative catalytic residue of the synthase domain, but observed no accumulation of (1,4)--glucan. Compared with wild-type Ags1p, this mutant Ags1p showed a markedly reduced ability to complement the cell lysis phenotype of the temperature-sensitive ags1-1 mutant. Therefore, we conclude that, in S. pombe, the production of (1,4)--glucan by the synthase domain of Ags1p is important for the biosynthesis of cell wall -glucan.
Original languageEnglish
Pages (from-to)18969-18979
JournalJournal of Biological Chemistry
Volume282
Issue number26
DOIs
Publication statusPublished - 2007

Keywords

  • multiple sequence alignment
  • coli glycogen-synthase
  • saccharomyces-cerevisiae
  • escherichia-coli
  • bacterial glycogen
  • schizosaccharomyces-pombe
  • aspergillus-fumigatus
  • phylogenetic trees
  • crystal-structure
  • chitin synthase

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