SGD Paper 
Okada H, et al. (2010) Multiple functional domains of the yeast l,3-beta-glucan synthase subunit Fks1p revealed by quantitative phenotypic analysis of temperature-sensitive mutants. Genetics 184(4):1013-24
Abstract: The main filamentous structural component of the cell wall of the yeast Saccharomyces cerevisiae is 1,3-beta-glucan, which is synthesized by a plasma membrane-localized enzyme called 1,3-beta-glucan synthase (GS). Here we analyzed the quantitative cell morphology and biochemical properties of ten different temperature-sensitive (ts) mutants of FKS1, a putative catalytic subunit of GS. To untangle their pleiotropic phenotypes, the mutants were classified into three functional groups. In the first group, mutants fail to synthesize 1,3-beta-glucan at the proper subcellular location, although GS activity is normal in vitro. In the second group, mutants have normal 1,3-beta-glucan content but are defective in polarized growth and endocytosis. In the third group, mutations in the putative catalytic domain of Fks1p result in a loss of the catalytic activity of GS. The differences between the three groups suggest that Fks1p consists of multiple domains which are required for cell wall construction and cellular morphogenesis.
| Status: Published | Type: Journal Article | PubMed ID: 20124029 |
Topics addressed in this paper
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| Topics | Genes linked to topics |
|---|---|
| FKS1 | |
| Function/Process |  |
| Genetic Interactions | |
| Mutants/Phenotypes | |
| Primary Literature | |
| Protein Sequence Features | |
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