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Absence of Gup1p in Saccharomyces cerevisiae results in defective cell wall composition, assembly, stability and morphology.
FEMS Yeast Res. 2006 Nov; 6(7):1027-38.FY

Abstract

Saccharomyces cerevisiae Gup1p and its homologue Gup2p, members of the superfamily of membrane-bound O-acyl transferases, were previously associated with glycerol-mediated salt-stress recovery and glycerol symporter activity. Several other phenotypes suggested Gup1p involvement in processes connected with cell structure organization and biogenesis. The gup1Delta mutant is also thermosensitive and exhibits an altered plasma membrane lipid composition. The present work shows that the thermosensitivity is independent of glycerol production and retention. Furthermore, the mutant grows poorly on salt, ethanol and weak carboxylic acids, suggestive of a malfunctioning membrane potential. Additionally, gup1Delta is sensitive to cell wall-perturbing agents, such as Calcofluor white, Zymolyase, lyticase and sodium dodecyl sulphate and exhibits a sedimentation/aggregation phenotype. Quantitative analysis of cell wall components yielded increased contents of chitin and beta-1,3-glucans and lower amounts of mannoproteins. Consistently, scanning electron microscopy showed a strikingly rough surface morphology of the mutant cells. These results suggest that the gup1Delta is affected in cell wall assembly and stability, although the Slt2p/MAP kinase from the PKC pathway was phosphorylated during hypo-osmotic shock to a normal extent. Results emphasize the pleiotropic nature of gup1Delta, and are consistent with a role of Gulp1p in connection with several pathways for cell maintenance and construction/remodelling.

Links

Publisher Full Text
academic.oup.com
onlinelibrary.wiley.com
onlinelibrary.wiley.com

Authors+Show Affiliations

Ferreira C
Carlsberg Laboratory, Copenhagen Valby, Denmark.
Silva S
No affiliation info available
van Voorst F
No affiliation info available
Aguiar C
No affiliation info available
Kielland-Brandt MC
No affiliation info available
Brandt A
No affiliation info available
Lucas C
No affiliation info available

MeSH

CaffeineCell WallMembrane GlycoproteinsMembrane Transport ProteinsMutationProtein Kinase CSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteinsbeta-Glucans

Pub Type(s)

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

Language

eng

PubMed ID

17042752

Citation

Ferreira, Célia, et al. "Absence of Gup1p in Saccharomyces Cerevisiae Results in Defective Cell Wall Composition, Assembly, Stability and Morphology." FEMS Yeast Research, vol. 6, no. 7, 2006, pp. 1027-38.
Ferreira C, Silva S, van Voorst F, et al. Absence of Gup1p in Saccharomyces cerevisiae results in defective cell wall composition, assembly, stability and morphology. FEMS Yeast Res. 2006;6(7):1027-38.
Ferreira, C., Silva, S., van Voorst, F., Aguiar, C., Kielland-Brandt, M. C., Brandt, A., & Lucas, C. (2006). Absence of Gup1p in Saccharomyces cerevisiae results in defective cell wall composition, assembly, stability and morphology. FEMS Yeast Research, 6(7), 1027-38.
Ferreira C, et al. Absence of Gup1p in Saccharomyces Cerevisiae Results in Defective Cell Wall Composition, Assembly, Stability and Morphology. FEMS Yeast Res. 2006;6(7):1027-38. PubMed PMID: 17042752.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Absence of Gup1p in Saccharomyces cerevisiae results in defective cell wall composition, assembly, stability and morphology. AU - Ferreira,Célia, AU - Silva,Sónia, AU - van Voorst,Frank, AU - Aguiar,Cristina, AU - Kielland-Brandt,Morten C, AU - Brandt,Anders, AU - Lucas,Cândida, PY - 2006/10/18/pubmed PY - 2006/12/9/medline PY - 2006/10/18/entrez SP - 1027 EP - 38 JF - FEMS yeast research JO - FEMS Yeast Res VL - 6 IS - 7 N2 - Saccharomyces cerevisiae Gup1p and its homologue Gup2p, members of the superfamily of membrane-bound O-acyl transferases, were previously associated with glycerol-mediated salt-stress recovery and glycerol symporter activity. Several other phenotypes suggested Gup1p involvement in processes connected with cell structure organization and biogenesis. The gup1Delta mutant is also thermosensitive and exhibits an altered plasma membrane lipid composition. The present work shows that the thermosensitivity is independent of glycerol production and retention. Furthermore, the mutant grows poorly on salt, ethanol and weak carboxylic acids, suggestive of a malfunctioning membrane potential. Additionally, gup1Delta is sensitive to cell wall-perturbing agents, such as Calcofluor white, Zymolyase, lyticase and sodium dodecyl sulphate and exhibits a sedimentation/aggregation phenotype. Quantitative analysis of cell wall components yielded increased contents of chitin and beta-1,3-glucans and lower amounts of mannoproteins. Consistently, scanning electron microscopy showed a strikingly rough surface morphology of the mutant cells. These results suggest that the gup1Delta is affected in cell wall assembly and stability, although the Slt2p/MAP kinase from the PKC pathway was phosphorylated during hypo-osmotic shock to a normal extent. Results emphasize the pleiotropic nature of gup1Delta, and are consistent with a role of Gulp1p in connection with several pathways for cell maintenance and construction/remodelling. SN - 1567-1356 UR - https://www.unboundmedicine.com/medline/citation/17042752/Absence_of_Gup1p_in_Saccharomyces_cerevisiae_results_in_defective_cell_wall_composition_assembly_stability_and_morphology_ L2 - https://academic.oup.com/femsyr/article-lookup/doi/10.1111/j.1567-1364.2006.00110.x DB - PRIME DP - Unbound Medicine ER -