The osmotolerant and cell wall properties of the two most studied wild-type Zygosaccharomyces rouxii strains (CBS 732 and ATCC 42981) were examined. Differences in their (1) tolerance to high salt content in the medium, (2) resistance to the lysing enzymes Lyticase and Zymolyase, (3) cell-wall polymer content and (4) cell wall micromorphology suggested that the less osmotolerant CBS 732 strain possesses a more rigid cell wall than the more osmotolerant ATCC 42981, whose cell wall seems to be more flexible and elastic.

• MeSH
• Antifungal Agents pharmacology   MeSH
• Cell Wall physiology   ultrastructure   MeSH
• Glucan Endo-1,3-beta-D-Glucosidase pharmacology   MeSH
• Adaptation, Physiological MeSH
• Saline Solution, Hypertonic metabolism   MeSH
• Multienzyme Complexes pharmacology   MeSH
• Osmolar Concentration MeSH
• Peptide Hydrolases pharmacology   MeSH
• Saccharomyces cerevisiae physiology   MeSH
• Zygosaccharomyces cytology   physiology   MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• Antifungal Agents MeSH
• Glucan Endo-1,3-beta-D-Glucosidase MeSH
• Saline Solution, Hypertonic MeSH
• lyticase MeSH Browser
• Multienzyme Complexes MeSH
• Peptide Hydrolases MeSH

Yarrowia lipolytica plasma-membrane Na+/H+ antiporter, encoded by the YlNHA2 gene, is a very efficient exporter of surplus sodium from the cytosol. Its heterologous expression in Saccharomyces cerevisiae wild-type laboratory strains increased their sodium tolerance more efficiently than the expression of ZrSod2-22 antiporter from the osmotolerant yeast Zygosaccharomvces rouxii.

• MeSH
• Antifungal Agents pharmacology   MeSH
• Gene Expression MeSH
• Fungal Proteins genetics   metabolism   MeSH
• Cloning, Molecular MeSH
• Sodium-Hydrogen Exchangers genetics   metabolism   MeSH
• Recombinant Proteins genetics   metabolism   MeSH
• Saccharomyces cerevisiae drug effects   genetics   growth & development   metabolism   MeSH
• Salts pharmacology   MeSH
• Yarrowia enzymology   genetics   MeSH
• Zygosaccharomyces enzymology   genetics   MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• Antifungal Agents MeSH
• Fungal Proteins MeSH
• Sodium-Hydrogen Exchangers MeSH
• Recombinant Proteins MeSH
• Salts MeSH

The Saccharomyces cerevisiae genome contains three genes encoding alkali metal cation/H+ antiporters (Nha1p, Nhx1p, Kha1p) that differ in cell localization, substrate specificity and physiological function. Systematic genome sequencing of other yeast species revealed highly conserved homologous ORFs in all of them. We compared the yeast sequences both at DNA and protein levels. The subfamily of yeast endosomal/prevacuolar Nhx1 antiporters is closely related to mammalian plasma membrane NHE proteins and to both plasma membrane and vacuolar plant antiporters. The high sequence conservation within this subfamily of yeast antiporters suggests that Nhx1p is of great importance in cell physiology. Yeast Kha1 proteins probably belong to the same subfamily as bacterial antiporters, whereas Nhal proteins form a distinct subfamily.

• MeSH
• DNA, Fungal analysis   MeSH
• Potassium-Hydrogen Antiporters chemistry   classification   genetics   MeSH
• Phylogeny MeSH
• Membrane Proteins chemistry   classification   genetics   MeSH
• Molecular Sequence Data MeSH
• Sodium-Hydrogen Exchangers chemistry   classification   genetics   MeSH
• Cation Transport Proteins chemistry   classification   genetics   MeSH
• Saccharomyces cerevisiae Proteins chemistry   classification   genetics   MeSH
• Amino Acid Sequence MeSH
• Sequence Analysis, DNA MeSH
• Sequence Homology, Amino Acid MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• DNA, Fungal MeSH
• Potassium-Hydrogen Antiporters MeSH
• KHA1 protein, S cerevisiae MeSH Browser
• Membrane Proteins MeSH
• Sodium-Hydrogen Exchangers MeSH
• NHA1 protein, S cerevisiae MeSH Browser
• NHX1 protein, S cerevisiae MeSH Browser
• Cation Transport Proteins MeSH
• Saccharomyces cerevisiae Proteins MeSH