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6414404 
Journal Article 
Identification of three mannoproteins in the cell wall of Saccharomyces cerevisiae 
van der Vaart, JM; Caro, LH; Chapman, JW; Klis, FM; Verrips, CT 
1995 
Yes 
Journal of Bacteriology
ISSN: 0021-9193
EISSN: 1098-5530 
177 
11 
3104-3110 
English 
7768807 
Three glucanase-extractable cell wall proteins from Saccharomyces cerevisiae were purified, and their N-terminal amino acid sequences were determined. With this information, we were able to assign gene products to three known open reading frames (ORFs). The N-terminal sequence of a 55-kDa mannoprotein corresponded with the product of ORF YKL096w, which we named CWP1 (cell wall protein 1). A 80-kDa mannoprotein was identified as the product of the TIP1 gene, and a 180-kDa mannoprotein corresponded to the product of the ORF YKL444, which we named CWP2. CWP1, TIP1, and CWP2 encode proteins of 239, 210, and 92 amino acids, respectively. The C-terminal regions of these proteins all consist for more than 40% of serine/threonine and contain putative glycosylphosphatidylinositol attachment signals. Furthermore, Cwp1p and Tip1p were shown to carry a beta 1,6-glucose-containing side chain. The cwp2 deletion mutant displayed an increased sensitivity to Congo red, calcofluor white, and Zymolyase. Electron microscopic analysis of the cwp2 deletion mutant showed a strongly reduced electron-dense layer on the outside of the cell wall. These results indicate that Cwp2p is a major constituent of the cell wall and plays an important role in stabilizing the cell wall. Depletion of Cwp1p or Tip1p also caused increased sensitivities to Congo red and calcofluor white, but the effects were less pronounced than for cwp2 delta. All three cell wall proteins show a substantial homology with Srp1p, which also appears to be localized in the cell wall. We conclude that these four proteins are small structurally related cell wall proteins. 
; Amino Acid Sequence; Base Sequence; Carrier Proteins; Cell Wall/chemistry; Cell Wall/ultrastructure; DNA Primers/chemistry; Fungal Proteins/genetics; Genes; Fungal; Glycoproteins; Glycoside Hydrolases/pharmacology; Glycosylphosphatidylinositols; Membrane Glycoproteins/genetics; Membrane Glycoproteins/physiology; Molecular Sequence Data; Mutagenesis; Insertional; Saccharomyces cerevisiae/chemistry; Saccharomyces cerevisiae/genetics; Saccharomyces cerevisiae Proteins; Sequence Deletion; Index Medicus/