Low external pH induces HOG1-dependent changes in the organization of the Saccharomyces cerevisiae cell wall

Mol Microbiol. 2001 Jan;39(2):469-79. doi: 10.1046/j.1365-2958.2001.02242.x.


Low environmental pH strongly affected the organization of the Saccharomyces cerevisiae cell wall, resulting in rapidly induced resistance to beta1,3-glucanase. At a molecular level, we found that a considerable amount of Cwp1p became anchored through a novel type of linkage for glycosylphosphatidylinositol (GPI)-dependent cell wall proteins, namely an alkali-labile linkage to beta1,3-glucan. This novel type of modification for Cwp1p did not require the presence of a GPI-derived structure connecting the protein with beta1,6-glucan. In addition, we found high levels of Cwp1p, which was double-anchored through both the novel alkali-sensitive bond to beta1,3-glucan and the alkali-resistant GPI-derived linkage to beta1,6-glucan. Further cell wall analyses demonstrated that Pir2p/Hsp150 and possibly other Pir cell wall proteins, which were already known to be linked to the beta1,3-glucan framework by an alkali-sensitive linkage, were also more efficiently retained in the cell wall at pH 3.5 than at pH 5.5. Consequently, the alkali-sensitive type of linkage of cell wall proteins to beta1,3-glucan was induced by low pH. The low pH-induced alterations in yeast cell wall architecture were demonstrated to be dependent on a functional HOG1 gene, but not on the Slt2p-mediated MAP kinase pathway. Consistent with this observation, DNA microarray studies revealed transcriptional induction of many known high-osmolarity glycerol (HOG) pathway-dependent genes, including four cell wall-related genes, namely CWP1, HOR7, SPI1 and YGP1.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Wall / chemistry
  • Cell Wall / genetics
  • Cell Wall / metabolism*
  • Chitin / analysis
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism*
  • Gene Expression Regulation, Fungal / genetics*
  • Glucan 1,3-beta-Glucosidase*
  • Glycoproteins*
  • Glycoside Hydrolases / pharmacology
  • Heat-Shock Proteins / genetics
  • Heat-Shock Proteins / metabolism
  • Hydrogen-Ion Concentration
  • Membrane Glycoproteins / genetics
  • Membrane Glycoproteins / metabolism
  • Mitogen-Activated Protein Kinases / genetics
  • Mitogen-Activated Protein Kinases / metabolism*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / growth & development*
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins*
  • Transcription, Genetic


  • CWP1 protein, S cerevisiae
  • Fungal Proteins
  • Glycoproteins
  • HSP150 protein, S cerevisiae
  • Heat-Shock Proteins
  • Membrane Glycoproteins
  • Saccharomyces cerevisiae Proteins
  • Chitin
  • HOG1 protein, S cerevisiae
  • Mitogen-Activated Protein Kinases
  • Glycoside Hydrolases
  • Glucan 1,3-beta-Glucosidase
  • beta-1,3-exoglucanase