Functional characterization of the Staphylococcus carnosus SecA protein in Escherichia coli and Bacillus subtilissecA mutant strains |
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Authors: | Michael Klein Jochen Meens Roland Freudl |
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Affiliation: | Institute of Molecular Cell Biology, BioCentrum, University of Amsterdam, Kruislaan 318, 1098 SM Amsterdam, The Netherlands |
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Abstract: | Abstract The cell wall of Candida albicans contains mannoproteins that are covalently associated with β-1,6-glucan. When spheroplasts were allowed to regenerate a new cell wall, initially non-glucosylated cell wall proteins accumulated in the medium. While the spheroplasts became osmotically stable, β-1,6-glucosylated proteins could be identified in their cell wall by SDS-extraction or β-1,3-glucanase digestion. At later stages of regeneration, β-1,3-glucosylated proteins were also found. Hence, incorporation of proteins into the cell wall is accompanied by extracellular coupling to β-1,6-/β-l,3-glucan. The SDS-extractable glucosylated proteins probably represent degradation products of wall proteins rather than their precursors. Tunicamycin delayed, but did not prevent the formation of β-1,6-glucosylated proteins, demonstrating that β-1,6-glucan is not attached to N -glycosidic side-chains of wall proteins. |
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Keywords: | β-1,6-glucan β-1,3-glucan Yeast Glycosyl-phosphatidyl-inositol (GPI)-anchor Glucomannoprotein Cell wall assembly Candida albicans |
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