The occurrence of glucosaminoglycan in the wall of Schizosaccharomyces pombe

Sietsma, J. H.; Wessels, J. G. H.

doi:10.1099/00221287-136-11-2261

Cited by 71 publications

(45 citation statements)

References 27 publications

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“…Third, the number of proteins we identified in the different species is comparable, although in Sz. pombe, consistent with the low amount of galactomannan in its walls (Sietsma and Wessels, 1990), we found only 33 putative GPI proteins. When the GPI algorithm was further tested on the rice blast fungus Magnaporthe grisea, we obtained a set of putative GPI proteins similar to the closely related N. crassa.…”

Section: Discussionsupporting

confidence: 76%

Genome‐wide identification of fungal GPI proteins

Groot

Hellingwerf

Klis

2003

Yeast

257

283

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Glycosylphosphatidylinositol-modified (GPI) proteins share structural features that allow their identification using a genomic approach. From the known S. cerevisiae and C. albicans GPI proteins, the following consensus sequence for the GPI attachment site and its downstream region was derived: This consensus sequence, which recognized known GPI proteins from various fungi, was used to screen the genomes of the yeasts S. cerevisiae, C. albicans, Sz. pombe and the filamentous fungus N. crassa for putative GPI proteins. The subsets of proteins so obtained were further screened for the presence of an N-terminal signal sequence for the secretion and absence of internal transmembrane domains. In this way, we identified 66 putative GPI proteins in S. cerevisiae. Some of these are known GPI proteins that were not identified by earlier genomic analyses, indicating that this selection procedure renders a more complete image of the S. cerevisiae GPI proteome. Using the same approach, 104 putative GPI proteins were identified in the human pathogen C. albicans. Among these were the proteins Gas/Phr, Ecm33, Crh and Plb, all members of GPI protein families that are also present in S. cerevisiae. In addition, several proteins and protein families with no significant homology to S. cerevisiae proteins were identified, including the cell wallassociated Als, Csa1/Rbt5, Hwp1/Rbt1 and Hyr1 protein families. In Sz. pombe, which has a low level of (galacto)mannan in the cell wall compared to C. albicans and S. cerevisiae, only 33 GPI candidates were identified and in N. crassa 97. BLAST searches revealed that about half of the putative GPI proteins that were identified in Sz. pombe and N. crassa are homologous to known or putative GPI proteins from other fungi. We conclude that our algorithm is selective and can also be used for GPI protein identification in other fungi.

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Section: Discussionsupporting

confidence: 76%

Genome‐wide identification of fungal GPI proteins

Groot

Hellingwerf

Klis

2003

Yeast

257

283

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“…For the class I tree, all the hyphomycetous and melanized Fungi Imperfecti are included in one branch, reflective of their possible loculoascomycetous affinities, whereas the remaining ascomycetous, ascocarpic fungi are included in another branch consisting of only the cleistothecial and the one perithecial species (9,17). While the exclusive clustering of the two ascocarpic ascomycetous groups is not apparent in the class II analysis, the clustering together of these same fungi with the hyphomycetous, melanized organisms in a single main branch that diverges from a second branch with the two Basidiomycetes and a third branch that encompasses the known or suspected ascosporic yeasts is still compatible with traditional fungal evolutionary schemes (18).…”

Section: Methodsmentioning

confidence: 99%

Classification of fungal chitin synthases.

Bowen

Chen-Wu

Momany

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

253

200

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Comparison of the chitin synthase genes of Saccharomyces cerevisiae CHSI and CHS2 with the Candida albicans CHSI gene (UDP-N-acetyl-D-glucosamine:chitin 4-j3-N-acetylglucosaminyltransferase, EC 2.4.1.16) revealed two small regions of complete amino acid sequence conservation that were used to design PCR primers. Fragments homologous to chitin synthase (=600 base pairs) were amplified from the genomic DNA of 14 fungal species. These fragments were sequenced, and their deduced amino acid sequences were aligned. With the exception of S. cerevisiae CHSI, the sequences fell into three distinct classes, which could represent separate functional groups. Within each class phylogenetic analysis was performed. Although not the major purpose of the investigation, this analysis tends to confirm some relationships consistent with current taxonomic groupings.Chitin, the ,/1-4-linked polymer of N-acetylglucosamine, is a fibrous cellulose-like polysaccharide that serves as the major cell wall/exoskeleton scaffolding in many species of fungi, arthropods, insects, and crustacea. In many yeasts chitin is used to maintain the structure of the mother-bud junction, whereas in filamentous fungi chitin is often the major supporting component of the cell wall.Early enzymatic studies in yeast and filamentous fungi showed that much of the chitin synthase activity was latent, requiring protease activation (1). Recent genetic and molecular studies in Saccharomyces cerevisiae suggest that this organism has at least two protease-activated chitin synthase zymogens as well as a more complex chitin synthase system that may not require protease activation (2).When the derived amino acid sequences of the two Sa. cerevisiae chitin synthase zymogens (from CHSJ and CHS2) were compared with the sequence of a closely related Candida albicans gene (for UDP-N-acetyl-D-glucosamine:chitin 4-f3-N-acetylglucosaminyltransferase, EC 2.4.1.16), it became clear that the enzymes contained a highly conserved sequence that possibly represents the catalytic region of the enzymes. We decided to use degenerate PCR primers that encoded short, completely conserved sequences within the three genes to probe genomic DNA from a variety offungi.** PCR-derived fragments were cloned into M13, and single nucleotide sequencing runs were used to classify the clones. Representative clones were then completely sequenced, and the deduced amino acid sequences were put into groups by the CLUSTAL program. The aligned DNA sequences within these groups, or classes, were analyzed further with the FITCH program.

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“…Schizosaccharomyces pombe contains a small amount of glucosamine, which is probably present as a b-(1,4)-linked glucosaminoglycan covalently linked to b-glucan in the cell wall, 3,4) but the role of chitin in S. pombe is not so clear.…”

Section: 2)mentioning

confidence: 99%