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  • Chemistry  (1)
  • Differential gene regulation  (1)
  • Hyphal-specific  (1)
  • 1
    ISSN: 1432-0983
    Keywords: Key wordsCandida albicans ; Gene family ; Hyphal-specific ; Differential gene regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The ALS1 (agglutinin-like sequence) gene of Candida albicans encodes a protein similar to alpha-agglutinin, a cell-surface adhesion glycoprotein of Saccharomyces cerevisiae (Hoyer et al. 1995). A central domain of a tandemly repeated 108-bp sequence is found in the ALS1 coding region. This tandem-repeat motif hybridizes to multiple C. albicans genomic DNA fragments, indicating the possibility of other ALS1-like genes in C. albicans (Hoyer et al. 1995). To determine if these fragments constitute a gene family, tandem-repeat-hybridizing genomic fragments were isolated from a fosmid library by PCR screening using primers based on the consensus tandem-repeat sequence of ALS1 (Hoyer et al. 1995). One group of fosmids, designated ALS3, encodes a gene with 81% identity to ALS1. The sequences of ALS1 and ALS3 are most conserved in the tandem-repeat domain and in the region 5′ of the tandem repeats. Northern-blot analysis using unique probes from the 3′ end of each gene demonstrated that ALS1 expression varies, depending on which C. albicans strain is examined, and that ALS3 is hyphal-specific. Both genes are found in a variety of C. albicans and C. stellatoidea strains examined. The predicted Als1p and Als3p exhibit features suggesting that both are cell-surface glycoproteins. Southern blots probed with conserved sequences from the region 5′ of the tandem repeats suggest that other ALS-like sequences are present in the C. albicans genome and that the ALS family may be larger than originally estimated.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0749-1581
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Methylmercuration of cytidine-3′-monophosphate is shown to occur at the N-3 site, resulting in a substantial upfield shift in the 15N resonance of this nitrogen. For guanosine-5′-monophosphate the 15N NMR data show N-1 to be the site of complexation of CH3Hg+ at pH 8. The large downfield shift observed for N-1 as a result of this binding is explained in terms of a concomitant deprotonation phenomenon. Changes in 13C NMR chemical shifts on methylmercuration are less pronounced, but consistent with these binding sites.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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