Document Detail


Enhanced levels of Pis1p (phosphatidylinositol synthase) improve the growth of Saccharomyces cerevisiae cells deficient in Rsp5 ubiquitin ligase.
MedLine Citation:
PMID:  16363994     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The Rsp5 ubiquitin ligase plays a role in many cellular processes including the biosynthesis of unsaturated fatty acids. The PIS1 (phosphatidylinositol synthase gene) encoding the enzyme Pis1p which catalyses the synthesis of phosphatidylinositol from CDP-diacyglycerol and inositol, was isolated in a screen for multicopy suppressors of the rsp5 temperature sensitivity phenotype. Suppression was allele non-specific. Interestingly, expression of PIS1 was 2-fold higher in the rsp5 mutant than in wild-type yeast, whereas the introduction of PIS1 in a multicopy plasmid increased the level of Pis1p 6-fold in both backgrounds. We demonstrate concomitantly that the expression of INO1 (inositol phosphate synthase gene) was also elevated approx. 2-fold in the rsp5 mutant as compared with the wild-type, and that inositol added to the medium improved growth of rsp5 mutants at a restrictive temperature. These results suggest that enhanced phosphatidylinositol synthesis may account for PIS1 suppression of rsp5 defects. Analysis of lipid extracts revealed the accumulation of saturated fatty acids in the rsp5 mutant, as a consequence of the prevention of unsaturated fatty acid synthesis. Overexpression of PIS1 did not correct the cellular fatty acid content; however, saturated fatty acids (C(16:0)) accumulated preferentially in phosphatidylinositol, and (wild-type)-like fatty acid composition in phosphatidylethanolamine was restored.
Authors:
Pawel Kaliszewski; Thierry Ferreira; Beata Gajewska; Anna Szkopinska; Thierry Berges; Teresa Zoładek
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Biochemical journal     Volume:  395     ISSN:  1470-8728     ISO Abbreviation:  Biochem. J.     Publication Date:  2006 Apr 
Date Detail:
Created Date:  2006-03-10     Completed Date:  2006-04-13     Revised Date:  2013-06-07    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  England    
Other Details:
Languages:  eng     Pagination:  173-81     Citation Subset:  IM    
Affiliation:
Department of Genetics, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland.
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MeSH Terms
Descriptor/Qualifier:
Catalysis
Cell Survival
Endosomal Sorting Complexes Required for Transport
Fatty Acids / metabolism
Gene Expression Regulation, Fungal
Genes, Suppressor
Inositol / pharmacology
Mutation / genetics
Myo-Inositol-1-Phosphate Synthase / genetics
Phenotype
Phosphatidylethanolamines / metabolism
Phosphatidylinositols / metabolism
Saccharomyces cerevisiae / cytology,  drug effects,  enzymology*,  growth & development*
Saccharomyces cerevisiae Proteins / genetics
Temperature
Transferases (Other Substituted Phosphate Groups) / genetics,  metabolism*
Ubiquitin-Protein Ligase Complexes / deficiency*,  genetics
Up-Regulation / genetics
Chemical
Reg. No./Substance:
0/Endosomal Sorting Complexes Required for Transport; 0/Fatty Acids; 0/Phosphatidylethanolamines; 0/Phosphatidylinositols; 0/Saccharomyces cerevisiae Proteins; 39382-08-6/phosphatidylethanolamine; 6917-35-7/Inositol; EC 2.7.8.-/Transferases (Other Substituted Phosphate Groups); EC 2.7.8.11/PIS1 protein, S cerevisiae; EC 5.5.1.4/Myo-Inositol-1-Phosphate Synthase; EC 6.3.2.19/RSP5 protein, S cerevisiae; EC 6.3.2.19/Ubiquitin-Protein Ligase Complexes
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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