Document Detail


Mutations in Fks1p affect the cell wall content of beta-1,3- and beta-1,6-glucan in Saccharomyces cerevisiae.
MedLine Citation:
PMID:  12185837     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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:
Gerrit J P Dijkgraaf; Mitsuhiro Abe; Yoshikazu Ohya; Howard Bussey
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Yeast (Chichester, England)     Volume:  19     ISSN:  0749-503X     ISO Abbreviation:  Yeast     Publication Date:  2002 Jun 
Date Detail:
Created Date:  2002-08-20     Completed Date:  2003-01-08     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  8607637     Medline TA:  Yeast     Country:  England    
Other Details:
Languages:  eng     Pagination:  671-90     Citation Subset:  IM    
Affiliation:
Department of Biology, McGill University, 1205 Dr. Penfield Ave., Montreal, Quebec, Canada H3A 1B1.
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MeSH Terms
Descriptor/Qualifier:
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:
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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