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

12 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

Fingerprint

Glucans
Schizosaccharomyces
Biosynthesis
Yeast
Cell Wall
Cells
Fungi
Starch Synthase
Glycogen Synthase
Amino Acid Motifs
Chitin
Structural integrity
Polysaccharides
Amino Acid Sequence
Maintenance
Phenotype
Amino Acids
Glucose
Mutation
Temperature

Keywords

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

Cite this

Vos, A., Dekker, N., Distel, B., Leunissen, J. A. M., & Hochstenbach, F. (2007). Role of the synthase domain of Ags1p in cell wall alfa-glucan biosynthesis in fission yeast. Journal of Biological Chemistry, 282(26), 18969-18979. https://doi.org/10.1074/jbc.M605147200
Vos, A. ; Dekker, N. ; Distel, B. ; Leunissen, J.A.M. ; Hochstenbach, F. / Role of the synthase domain of Ags1p in cell wall alfa-glucan biosynthesis in fission yeast. In: Journal of Biological Chemistry. 2007 ; Vol. 282, No. 26. pp. 18969-18979.
@article{7708056750524fc7a8c89f8dff4e2139,
title = "Role of the synthase domain of Ags1p in cell wall alfa-glucan biosynthesis in fission yeast",
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.",
keywords = "multiple sequence alignment, coli glycogen-synthase, saccharomyces-cerevisiae, escherichia-coli, bacterial glycogen, schizosaccharomyces-pombe, aspergillus-fumigatus, phylogenetic trees, crystal-structure, chitin synthase",
author = "A. Vos and N. Dekker and B. Distel and J.A.M. Leunissen and F. Hochstenbach",
year = "2007",
doi = "10.1074/jbc.M605147200",
language = "English",
volume = "282",
pages = "18969--18979",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology",
number = "26",

}

Vos, A, Dekker, N, Distel, B, Leunissen, JAM & Hochstenbach, F 2007, 'Role of the synthase domain of Ags1p in cell wall alfa-glucan biosynthesis in fission yeast', Journal of Biological Chemistry, vol. 282, no. 26, pp. 18969-18979. https://doi.org/10.1074/jbc.M605147200

Role of the synthase domain of Ags1p in cell wall alfa-glucan biosynthesis in fission yeast. / Vos, A.; Dekker, N.; Distel, B.; Leunissen, J.A.M.; Hochstenbach, F.

In: Journal of Biological Chemistry, Vol. 282, No. 26, 2007, p. 18969-18979.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Role of the synthase domain of Ags1p in cell wall alfa-glucan biosynthesis in fission yeast

AU - Vos, A.

AU - Dekker, N.

AU - Distel, B.

AU - Leunissen, J.A.M.

AU - Hochstenbach, F.

PY - 2007

Y1 - 2007

N2 - 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.

AB - 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.

KW - multiple sequence alignment

KW - coli glycogen-synthase

KW - saccharomyces-cerevisiae

KW - escherichia-coli

KW - bacterial glycogen

KW - schizosaccharomyces-pombe

KW - aspergillus-fumigatus

KW - phylogenetic trees

KW - crystal-structure

KW - chitin synthase

U2 - 10.1074/jbc.M605147200

DO - 10.1074/jbc.M605147200

M3 - Article

VL - 282

SP - 18969

EP - 18979

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 26

ER -