| Mutations in Fks1p affect the cell wall content of beta-1,3- and beta-1,6-glucan in Saccharomyces cerevisiae. | |
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MedLine Citation:
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PMID: 12185837 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Fks1p and Fks2p are related proteins thought to be catalytic subunits of the beta-1,3-glucan synthase. Analysis of fks1 delta mutants showed a partial K1 killer toxin-resistant phenotype and a 30% reduction in alkali-soluble beta-1,3-glucan that was accompanied by a modest reduction in beta-1,6-glucan. The gas1 delta mutant lacking a 1,3-beta-glucanosyltransferase displayed a similar reduction in alkali-soluble beta-1,3-glucan but did not share the beta-1,6-glucan defect, indicating that beta-1,6-glucan reduction is not a general phenotype among beta-1,3-glucan biosynthetic mutants. Overexpression of FKS2 suppressed the killer toxin phenotype of fks1 delta mutants, implicating Fks2p in the biosynthesis of the residual beta-1,6-glucan present in fks1 delta cells. In addition, eight out of 12 fks1ts fks2 delta mutants had altered beta-glucan levels at the permissive temperature: the partial killer resistant FKS1F1258Y N1520D allele was severely affected in both polymers and displayed a 55% reduction in beta-1,6-glucan, while the in vitro hyperactive allele FKS1T605I M761T increased both beta-glucan levels. These beta-1,6-glucan phenotypes may be due to altered availability of, and structural changes in, the beta-1,3-glucan polymer, which might serve as a beta-1,6-glucan acceptor at the cell surface. Alternatively, Fks1p and Fks2p could actively participate in the biosynthesis of both polymers as beta-glucan transporters. We analysed Fks1p and Fks2p in beta-1,6-glucan deficient mutants and found that they were mislocalized and that the mutants had reduced in vitro glucan synthase activity, possibly contributing to the observed beta-1,6-glucan defects. |
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Authors:
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Gerrit J P Dijkgraaf; Mitsuhiro Abe; Yoshikazu Ohya; Howard Bussey |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Yeast (Chichester, England) Volume: 19 ISSN: 0749-503X ISO Abbreviation: Yeast Publication Date: 2002 Jun |
Date Detail:
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Created Date: 2002-08-20 Completed Date: 2003-01-08 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 8607637 Medline TA: Yeast Country: England |
Other Details:
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Languages: eng Pagination: 671-90 Citation Subset: IM |
Affiliation:
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Department of Biology, McGill University, 1205 Dr. Penfield Ave., Montreal, Quebec, Canada H3A 1B1. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Blotting, Western Cell Wall / genetics, metabolism DNA, Fungal / genetics, metabolism Echinocandins Epitopes Fungal Proteins / genetics*, metabolism Gene Expression Regulation, Enzymologic Gene Expression Regulation, Fungal Glucans / biosynthesis* Glucosyltransferases / metabolism Killer Factors, Yeast Membrane Proteins / genetics*, metabolism Mutation / genetics Mycotoxins / metabolism Polymerase Chain Reaction Saccharomyces cerevisiae / enzymology, genetics*, metabolism Saccharomyces cerevisiae Proteins* beta-Glucans* |
| Chemical | |
Reg. No./Substance:
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0/DNA, Fungal; 0/Echinocandins; 0/Epitopes; 0/Fungal Proteins; 0/Glucans; 0/K1 killer toxin; 0/Killer Factors, Yeast; 0/Membrane Proteins; 0/Mycotoxins; 0/Saccharomyces cerevisiae Proteins; 0/beta-Glucans; 37361-00-5/beta-1,6-glucan; 9051-97-2/beta-1,3-glucan; EC 2.4.1.-/Glucosyltransferases; EC 2.4.1.-/glucan synthase; EC 2.4.1.34/FKS1 protein, S cerevisiae; EC 2.4.1.34/FKS2 protein, S cerevisiae |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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