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.
journal_name
Mol Microbioljournal_title
Molecular microbiologyauthors
Zhu YS,Zhang XY,Cartwright CP,Tipper DJdoi
10.1111/j.1365-2958.1992.tb01496.xsubject
Has Abstractpub_date
1992-02-01 00:00:00pages
511-20issue
4eissn
0950-382Xissn
1365-2958journal_volume
6pub_type
杂志文章abstract::N-glycosylation in the endoplasmic reticulum is an essential protein modification and highly conserved in evolution from yeast to man. Defects of N-glycosylation in humans lead to congenital disorders. The pivotal step of this pathway is the transfer of the evolutionarily conserved lipid-linked core-oligosaccharide to...
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journal_title:Molecular microbiology
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journal_title:Molecular microbiology
pub_type: 杂志文章
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pub_type: 评论,杂志文章
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更新日期:2015-09-01 00:00:00