Processing of predicted substrates of fungal Kex2 proteinases from Candida albicans, C. glabrata, Saccharomyces cerevisiae and Pichia pastoris |
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Authors: | Oliver Bader Yannick Krauke Bernhard Hube |
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Affiliation: | (1) FG16,, Robert Koch-Institut, Nordufer 20, D-13353, Berlin, Germany;(2) Institut fr Medizinische Mikrobiologie, Universitt Gttingen,, Kreuzbergring 57, D-37075, Gttingen, Germany;(3) Dept. Membrane Transport, Institute of Physiology AS CR v.v.i.,, Videnska 1083, 142 20 Prague 4, Czech Republic;(4) Department of Microbial Pathogenicity, Leibniz Institute for Natural Product Research and Infection Biology Hans Knoell Institute, Beutenbergstrasse 11a, D-07745 Jena, Germany;(5) Friedrich-Schiller-University Jena, Jena, Germany |
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Abstract: | Background Kexin-like proteinases are a subfamily of the subtilisin-like serine proteinases with multiple regulatory functions in eukaryotes. In the yeast Saccharomyces cerevisiae the Kex2 protein is biochemically well investigated, however, with the exception of a few well known proteins such as the α-pheromone precursors, killer toxin precursors and aspartic proteinase propeptides, very few substrates are known. Fungal kex2 deletion mutants display pleiotropic phenotypes that are thought to result from the failure to proteolytically activate such substrates. |
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