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Mutations in Fks1p affect the cell wall content of beta-1,3- and beta-1,6-glucan in Saccharomyces cerevisiae.
Yeast. 2002 Jun 15; 19(8):671-90.Y

Abstract

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.

Authors+Show Affiliations

Dijkgraaf GJ
Department of Biology, McGill University, 1205 Dr. Penfield Ave., Montreal, Quebec, Canada H3A 1B1.
Abe M
No affiliation info available
Ohya Y
No affiliation info available
Bussey H
No affiliation info available

MeSH

Blotting, WesternCell WallDNA, FungalEchinocandinsEpitopesFungal ProteinsGene Expression Regulation, EnzymologicGene Expression Regulation, FungalGlucansGlucosyltransferasesKiller Factors, YeastMembrane ProteinsMutationMycotoxinsPolymerase Chain ReactionSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteinsbeta-Glucans

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

12185837

Citation

Dijkgraaf, Gerrit J P., et al. "Mutations in Fks1p Affect the Cell Wall Content of Beta-1,3- and Beta-1,6-glucan in Saccharomyces Cerevisiae." Yeast (Chichester, England), vol. 19, no. 8, 2002, pp. 671-90.
Dijkgraaf GJ, Abe M, Ohya Y, et al. Mutations in Fks1p affect the cell wall content of beta-1,3- and beta-1,6-glucan in Saccharomyces cerevisiae. Yeast. 2002;19(8):671-90.
Dijkgraaf, G. J., Abe, M., Ohya, Y., & Bussey, H. (2002). Mutations in Fks1p affect the cell wall content of beta-1,3- and beta-1,6-glucan in Saccharomyces cerevisiae. Yeast (Chichester, England), 19(8), 671-90.
Dijkgraaf GJ, et al. Mutations in Fks1p Affect the Cell Wall Content of Beta-1,3- and Beta-1,6-glucan in Saccharomyces Cerevisiae. Yeast. 2002 Jun 15;19(8):671-90. PubMed PMID: 12185837.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Mutations in Fks1p affect the cell wall content of beta-1,3- and beta-1,6-glucan in Saccharomyces cerevisiae. AU - Dijkgraaf,Gerrit J P, AU - Abe,Mitsuhiro, AU - Ohya,Yoshikazu, AU - Bussey,Howard, PY - 2002/8/21/pubmed PY - 2003/1/9/medline PY - 2002/8/21/entrez SP - 671 EP - 90 JF - Yeast (Chichester, England) JO - Yeast VL - 19 IS - 8 N2 - 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. SN - 0749-503X UR - https://www.unboundmedicine.com/medline/citation/12185837/Mutations_in_Fks1p_affect_the_cell_wall_content_of_beta_13__and_beta_16_glucan_in_Saccharomyces_cerevisiae_ DB - PRIME DP - Unbound Medicine ER -