Mutational analysis of the functional domains of yeast K1 killer toxin.
To determine the functional domains of K1 killer toxin, we analyzed the phenotypes of a set of mutations throughout regions encoding the alpha- and beta-toxin subunits that allow secretion of mutant toxins. A range of techniques have been used to examine the ability of mutant toxins to bind to beta-glucan cell wall receptor and to form lethal ion channels. Our results indicate that both the alpha and beta subunits are involved in beta-glucan receptor binding. Defects in ion channel formation and toxin immunity are confined to the hydrophobic alpha subunit of the toxin.
Department of Biology, McGill University, Montreal, Quebec, Canada.
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D001483:Base Sequence; D002473:Cell Wall / Q000378:metabolism; D003001:Cloning, Molecular; D004252:DNA Mutational Analysis; D005656:Fungal Proteins / Q000235:genetics; D007473:Ion Channels / Q000235:genetics*; D055646:Killer Factors, Yeast; D008969:Molecular Sequence Data; D009183:Mycotoxins / Q000235:genetics* / Q000378:metabolism; D009841:Oligonucleotides; D011485:Protein Binding; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins; D013329:Structure-Activity Relationship
D005656:Fungal Proteins; D007473:Ion Channels; C527157:KHR1 protein, S cerevisiae; D055646:Killer Factors, Yeast; D009183:Mycotoxins; D009841:Oligonucleotides; D029701:Saccharomyces cerevisiae Proteins