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  • Ascomycete  (2)
  • Candida albicans  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Molecular genetics and genomics 250 (1996), S. 214-222 
    ISSN: 1617-4623
    Schlagwort(e): Key words Neurospora ; Ascomycete ; Fungal cell wall
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract  In Saccharomyces cerevisiae, most of the cellular chitin is produced by chitin synthase III, which requires the product encoded by the CSD2/CAL1/ DIT101/KT12 gene. We have identified, isolated and structurally characterized a CSD2/CAL1/DIT101/KT12 homologue in the filamentous ascomycete Neurospora crassa and have used a “reverse genetics” approach to determine its role in vivo. The yeast gene was used as a heterologous probe for the isolation of a N. crassa gene (designated chs-4) encoding a polypeptide belonging to a class of chitin synthases which we have designated class IV. The predicted polypeptide encoded by this gene is highly similar to those of S. cerevisiae and Candida albicans. N. crassa strains in which chs-4 had been inactivated by the Repeat-Induced Point mutation (RIP) process grew and developed in a normal manner under standard growth conditions. However, when grown in the presence of sorbose (a carbon source which induces morphological changes accompanied by elevated chitin content), chitin levels in the chs-4 RIP strain were significantly lower than those observed in the wild type. We suggest that CHS4 may serve as an auxiliary enzyme in N. crassa and that, in contrast to yeasts, it is possible that filamentous fungi may have more than one class IV chitin synthase.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Molecular genetics and genomics 250 (1996), S. 214-222 
    ISSN: 1617-4623
    Schlagwort(e): Neurospora ; Ascomycete ; Fungal cell wall
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract InSaccharomyces cerevisiae, most of the cellular chitin is produced by chitin synthase III, which requires the product encoded by theCSD2/CAL1/DIT101/KT12 gene. We have identified, isolated and structurally characterized aCSD2/CAL1/DIT101/KT12 homologue in the filamentous ascomyceteNeurospora crassa and have used a “reverse genetics” approach to determine its role in vivo. The yeast gene was used as a heterologous probe for the isolation of aN. crassa gene (designatedchs-4) encoding a polypeptide belonging to a class of chitin synthases which we have designated class IV. The predicted polypeptide encoded by this gene is highly similar to those ofS. cerevisiae andCandida albicans. N. crassa strains in whichchs-4 had been inactivated by the Repeat-Induced Point mutation (RIP) process grew and developed in a normal manner under standard growth conditions. However, when grown in the presence of sorbose (a carbon source which induces morphological changes accompanied by elevated chitin content), chitin levels in thechs-4 RIP strain were significantly lower than those observed in the wild type. We suggest that CHS4 may serve as an auxiliary enzyme inN. crassa and that, in contrast to yeasts, it is possible that filamentous fungi may have more than one class IV chitin synthase.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 3
    Digitale Medien
    Digitale Medien
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 501-504 
    ISSN: 0749-503X
    Schlagwort(e): Candida albicans ; chitinase ; yeast ; nucleotide sequencing ; Life Sciences ; Life Sciences (general)
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie
    Notizen: Here we report the complete nucleotide sequence of a third chitinase gene (CHT1) from the dimorphic human pathogen Candida albicans. The deduced amino acid (aa) sequence of Cht1 consists of 416 aa and displays 36% protein sequence similarity to chitinases Cht2 and Cht3, from C. albicans. Interestingly the domain structure of Cht1 is truncated when compared to the other chitinases of C. albicans and lacks a Ser/Thr-rich region. The sequence data will appear in the GenBank Nucleotide Sequence Data Library under the accession number U36490.
    Zusätzliches Material: 3 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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