| Literature DB >> 1560780 |
Y S Zhu1, X Y Zhang, C P Cartwright, D J Tipper.
Abstract
The K1 killer toxin of Saccharomyces cerevisiae consists of 103- and 83-residue alpha and beta components whose derivation, from a 316-residue precursor preprotoxin, requires processing at the alpha N-terminus (after ProArg-44), the alpha C-terminus (after ArgArg-149) and at the beta N-terminus (after LysArg-233). These processing events occur after translocation to the Golgi and have been investigated using beta-lactamase fusions. Signal peptidase cleavage of the precursor, predicted to occur after Ala-26, was confirmed by N-terminal sequence analysis of Ala-34 and Ile-52 fusions. Cleavage at all of the other predicted processing sites, including ProArg-44, is dependent on activity of the Kex2 protease. A fourth Kex2-dependent cleavage occurs at LysArg-188. Implications for the specificity of Kex2 cleavage and preprotoxin processing are discussed.Entities:
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Year: 1992 PMID： 1560780 DOI： 10.1111/j.1365-2958.1992.tb01496.x
Source DB: PubMed Journal: Mol Microbiol ISSN： 0950-382X Impact factor: 3.501